\r\n\tfires. Infrastructure development and human settlements are blocking migratory corridors, thus suppressing their critical role of maintaining the ecological processes including allowing for the movement of animals and the continuation of viable populations. Human-wildlife conflicts are growing as a \r\n\tresult of population growth and, therefore, increasing demand for natural resources and increased proximity to wildlife.
\r\n
\r\n\tExotic and invasive species are outcompeting native species for resources or habitat and altering community structure with detrimental consequences on native species. \r\n\tImpacts of climate change on wildlife are increasing and manifested through habitat destruction, increased human-wildlife conflicts, diseases and death of wild animals. Illegal and unsustainable hunting is increasing to cater for subsistence and commercial demands within and outside the national boundaries, thus leading to a dramatic drop of populations or extinction of species.
\r\n
\r\n\tChapters presented in this book attempt to respond to four questions: How do the political, economic, social, ecological and technological changes influence the survival of wildlife? How do these changes shape the management policies and approaches? How effective are the existing strategies and options to coping with these changes? Which are the possible options to address these changes and secure a future for wildlife?
\r\n
\r\n\tThis Book serves as an important platform for information and experience sharing among the scientists, academicians, students, conservationists and policy-makers from different parts of the world.
",isbn:"978-1-83880-976-8",printIsbn:"978-1-83880-975-1",pdfIsbn:"978-1-83880-977-5",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"a27827009edc70af81e12c10aa3e51dd",bookSignature:"Prof. Jafari Kideghesho",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/8834.jpg",keywords:"Wildlife, Conservation, Poaching, Law Enforcement, Protected Areas, Wildlife Habitats, Migratory Corridors, Wildlife Diseases, Invasive Species, Wildlife Utilization, Human-Wildlife Interactions, Wildlife Conservation Policies",numberOfDownloads:233,numberOfWosCitations:0,numberOfCrossrefCitations:0,numberOfDimensionsCitations:0,numberOfTotalCitations:0,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"May 15th 2020",dateEndSecondStepPublish:"June 5th 2020",dateEndThirdStepPublish:"August 4th 2020",dateEndFourthStepPublish:"October 23rd 2020",dateEndFifthStepPublish:"December 22nd 2020",remainingDaysToSecondStep:"9 months",secondStepPassed:!0,currentStepOfPublishingProcess:5,editedByType:null,kuFlag:!1,biosketch:"Dr. Kideghesho served as a Deputy Director of Wildlife Division in Tanzania's Ministry of Natural Resources and Tourism for two years (2012-2014). He is an active supporter of academic efforts within and outside Tanzania through teaching and serving as external examiner at different universities.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"280695",title:"Prof.",name:"Jafari R.",middleName:null,surname:"Kideghesho",slug:"jafari-r.-kideghesho",fullName:"Jafari R. Kideghesho",profilePictureURL:"https://mts.intechopen.com/storage/users/280695/images/system/280695.jpg",biography:"Prof. Jafari R Kideghesho is the current Rector of the College of African Wildlife Management (CAWM), Mweka and a seasoned expert in Conservation Biology. He obtained his PhD from Norwegian University of Science and Technology (NTNU), Trondheim Norway in 2006, MSc (Conservation Biology) from Durrell Institute of Conservation and Ecology (DICE) of the University of Kent at Canterbury, UK in 1996 and a BSc. (Agriculture) from Sokoine University of Agriculture (SUA), Tanzania in 1993. He has worked for over 25 years in various positions in the Wildlife Sector as Assistant Lecturer at CAWM, Mweka, Lecturer, Senior Lecturer and Associate Professor at the Department of Wildlife Management at SUA and Assistant Director (Wildlife Utilization) in the Ministry of Natural Resources and Tourism. Kideghesho has been involved in over 20 local and international professional committees and organizations as a member, moderator, external examiner and a reviewer of scientific journals. He has published about 60 scientific articles and book chapters in peer reviewed journals and edited books, several articles in Conference Proceedings and 9 in Tanzania’s popular Wildlife Magazine. He is an editor of a book titled - Wildlife Management: Failures, Successes and Prospects. 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1. Introduction
Soybean meal is considered the “gold standard” among intact protein sources used in the feed industry (Cromwell, 1999). It has an excellent amino acid profile that complements cereal grains in diet formulation, as methionine is typically the only limiting amino acid for poultry. Soybean meal is characterized as either from dehulled beans or beans having hulls (NRC, 1994). Dehulled soybean meal has a higher composition of crude protein, amino acids and metabolizable energy than soybean meal produced from soybeans having hulls (NRC, 1994); Soybean meal is known to vary in amino acid composition among samples. Geographical location of soybean production, soybean variety, and processing methods are factors known to influence variability of crude protein and amino acid composition of soybean meal (Parsons et al., 1991, 2000; de Coca-Sinova, 2008, 2010; Baker et al., 2011). de Coca-Sinova (2008) evaluated amino acid composition of soybean meal samples obtained from Argentina, Brazil, Spain, and the United States. Crude protein content varied from 45.2 to 50.6% with lysine expressed as a percent of crude protein ranging from 5.51 to 6.26%. Samples from Spain had the highest crude protein content, whereas lysine expressed as a percentage of crude protein was the highest for samples obtained in the United States.
Moreover, soybean varieties are being selected to contain higher amino acid concentrations than conventional soybean varieties resulting in soybean meals having more balanced amino acid content for swine and poultry diets (Baker and Stein, 2009; Baker et al., 2011). Baker et al. (2011) reported high protein soybean meal having a crude protein and lysine composition of 54.86 and 3.56% compared with conventional soybean meal containing crude protein and lysine contents of 47.47 and 3.14%. Soybean meal is known to vary in crude protein and amino acid content among soybean production years and using current amino acid data bases of soybean meal composition are important to avoid variability in diet formulation with swine and poultry (Table 1).
Amino acids originating from intact protein sources are not digested and absorbed with 100% efficiency. Formulating diets on a digestible amino acid basis is increasing around the globe and this formulation strategy allows for the use of lower cost feed ingredients that may contain amino acids that are less available to the animal while minimizing nitrogen excretion. Digestible amino acid composition is calculated by multiplying a digestible coefficient by amino acid total composition. Digestible coefficient is the digestibility percentage of an amino acid in a specific feed ingredient or a complete diet. In poultry, amino acid digestibility coefficients for feed ingredients are typically determined using a true digestibility assay with cecectomized roosters (Parsons, 1986) or standardized amino acid assay using broilers (Lemme et al., 2004). Amino acid digestibility coefficients have been reported to be higher with cecectomized roosters compared with using broilers (Garcia et al., 2007; Adedokun et al., 2007). Amino acid digestibility assays are highly variable and a large number of assays are needed for specific feedstuffs to generate accurate digestibility coefficients. Amino acid digestibility coefficients for soybean meal have been found to range from 82 to 93% (Table 2).
Sriperm et al., 20111
Evonik2
Novus3
Lysine
3.23±0.11
2.95±0.07
2.96±0.15
Methionine
0.77±0.04
0.64±0.01
0.64±0.04
Cysteine
0.69±0.04
0.70±0.02
0.64±0.05
Arginine
3.73±0.19
3.48±0.11
3.41±0.17
Tryptophan
0.68±0.68
0.64±0.01
0.66±0.04
Isoleucine
2.31±0.09
2.15±0.06
2.20±0.13
Leucine
3.90±0.15
3.61±0.09
3.63±0.17
Valine
2.41±0.09
2.25±0.05
2.33±0.13
Histidine
1.35±0.07
1.26±0.03
1.25±0.06
Phenylalanine
2.65±0.02
2.40±0.06
2.37±0.12
Sample size
225
457
75
Table 1.
Essential amino acid composition (%) of soybean meal obtained from various regions of the United States. 1Values are expressed on a dry matter basis as average ± SD and were determined from samples analyzed in 2009 at Ajinomoto Heartland LLC’s amino acid laboratory. 2Values are expressed on a “as-is basis” as average ± SD and were determined from samples analyzed in 2010 at Evonik’s amino acid laboratory. 3Values are expressed on a “as-is basis” as average ± SD and were determined from samples analyzed in 2010 at Novus International Inc., amino acid laboratory.
True Digestibility1
Standardized Assay2
Lysine
91±2.8
90
Methionine
92±2.5
91
Cysteine
84±5.1
82
Threonine
88±3.4
85
Arginine
93±2.8
93
Tryptophan
89±4.8
89
Isoleucine
92±3.3
89
Leucine
92±2.2
89
Valine
91±2.5
88
Histidine
90±6.5
92
Phenylalanine
92±3.7
88
Sample size
88
37
Table 2.
Digestible amino acid coefficients (%) of soybean meal. 1Values are expressed as average ± SD of 88 samples from Ajinomoto Heartland. 2Values are expressed as average of 35 samples from Evonik.
2. Soybean meal in poultry and swine feeds
Soybean meal is the most commonly-used source of protein for poultry and swine feeds in the world, with 67% of the animal feed market (Pettigrew et al., 2002). In order for a feed ingredient to be considered an important component of an industry feeding program, it must have several fundamental qualities. First, it must provide one or more important nutrients. Second, it must be available in amounts that allow it to be used regularly and on a large scale. Third, it must be cost effective to use. Soybean meal abundantly fits into this category as a high-protein product with good amino acid balance that is highly digestible. It is available in large quantities year round and has had most of the associated antinutritional compounds inactivated. Interestingly, antinutritional factors in soybeans are relatively easy to inactivate and are reduced substantially by normal soybean processing. This is in contrast to many of the other commonly-used plant proteins that have non-labile antinutritional factors (Pettigrew et al., 2002).
In the early years of compound feed production, grain products were paired with animal protein meals that provided a natural balance of vitamins and minerals in addition to protein. As animal protein products such as fishmeal became more expensive, and synthetic sources of vitamins (particularly vitamin B12) were developed, soybean meal captured a larger portion of the animal feed protein market. Modern feed formulation programs further increased the demand for soybean meal as the principle protein source as least cost diet formulation became more common.
Worldwide, nearly 2/3 of the protein sources used in animal feeds come from soybean meal, with canola meal, cottonseed meal and sunflower meal providing additional plant protein sources. In the United States, plant protein source usage in animal feeds is primarily (92%) soybean meal. Over half of the soybean meal produced in the United States is fed to poultry (Waldroup and Smith, 1999). Approximately 66% of protein in broiler feeds comes from soybean meal. With the development of reasonably-priced synthetic methionine sources, feed manufacturers are now able to produce relatively simple feeds based on a combination of corn and soybean meal with supplementation of minerals, vitamins and methionine. Swine account for 27% of the soybean meal used in animal feeds in the United States. Soy protein’s digestibility, combined with a relative abundance of lysine, which is the first limiting amino acid in swine feeds, make soybean meal an excellent protein source for swine.
Most areas of swine and poultry production have economical access to soybean meal for compounding animal feeds. In some places, however, local access to soybeans has led to interest in the processing of full fat soybeans meals for local usage. Full fat soybean meal, often an extruded product, has the advantage of higher energy values due to the full complement of oil in the native seeds as compared to commercial soybean meal, which has had most of the oil extracted for sale (Reese and Bitney, 2000). Other advantages include: 1) the addition of fat to a feed in a more easily-handled granular form and 2) the addition of fat to a feed in a form that is less likely to reduce pellet quality (Waldroup, 1985).
Performance results indicated that there was significant variation in the nutrient content from various batches of extruded soybean meals (Reese and Bitney, 2000). The authors concluded that it would be difficult to compare extruded soybean meal to regularly-processed soybean meal for this reason. It would be wise if considering these products to do extra nutrient analysis. Numerous research groups have explored the use of full fat soybean meals in poultry feeds as well (Waldroup, 1985). Extruded full fat soybean meals have seen limited use, although dry roasting, followed by grinding, has also been tested. Waldroup and Cotton (1974) determined the levels of full fat soybean meal that could be included in mash broiler feeds before performance suffered (less than 25%). Higher levels could be utilized in pelleted broiler feeds because the pelleting process causes more cell wall disruption and increases the digestibility of full fat soybean meal products (Waldroup and Cotton, 1974).
Soybean geneticists are continually improving productivity characteristics of soybeans for crop production. Additionally, efforts have been underway for some time to enhance the quality of soybeans in relation to animal feeding of soybean meal (Bajjaleih, 2002). Areas of interest include increasing levels of sulfur containing amino acids, increasing the proportion of soybean meal phosphorus that is available for digestion (reducing phytate-bound phosphorus) and increasing energy availability through selection away from carbohydrate fractions of low availability to monogastrics.
3. Protein digestion
Dietary protein consists of complex polypeptides, which must be cleaved into dipeptides and amino acids to facilitate absorption. In poultry, the crop, proventriculus, gizzard, pancreas, and small intestine have an active role in protein digestion (Moran, 1982). Proteolysis is the first stage of digestion and it occurs in the proventriculus and gizzard (Hill, 1971). The contents found in the proventriculus and gizzard have a pH of 1.80 and 2.50, respectively, which is relatively lower than the crop, small intestine, cecum, and cloaca (Figure 1). This low pH is central to gastric digestion. The Proventriculus is the site for pepsin and HCl production and contains gastric glands located in the mucosa (Toner, 1963). At low pH, protein denaturation occurs through unfolding of proteins and cleavage of peptide bonds by pepsin, which is an endopeptidase.
Figure 1.
pH of the contents in the digestive tract of poultry (Herpol and Van Grembergen, 1967)
One of the functions of the pancreas is to supply digestive enzymes for protein digestion (Brody, 1994). Trypsin, chymotrypsin A, chymotrypsin B, proelastase, and carboxypeptidase are produced by the pancreas and these enzymes are endopeptidases with the exception of carboxypeptidase (Brody, 1994). Pancreatic enzymes play a central role in protein digestion in the small intestine by breaking down polypeptides into oligopeptides (Alpers, 1994; Lowe, 1994). Approximately 13 peptidases are present in the brush border membrane or the cytoplasm of the small intestine that breakdown oligopeptides into dipeptides and amino acids (Alpers, 1994). The resulting dipeptides and amino acids are absorbed in the small intestine for the synthesis of body proteins.
Soybean meal that has been underprocessed contains trypsin inhibitors, which are antinutritional factors. These proteins bind to trypsinogen and chymotrypsinogen preventing the conversion into their active forms limiting protein digestion. A detailed description of trypsin inhibitors will be discussed in the following section.
4. Trypsin inhibtor in soybean meal and protein digestion
Growth depression effects due to antinutritional factors present in soybeans have been well-documented for more than half a century (Ham et al., 1945; Chernick et al., 1948; Liener, 1953; Lyman and Lepkovsky, 1957; Gestetner et al., 1966). Trypsin inhibitor is the primary antinutritional factor in soybean meal (Araba and Dale, 1990a,b; Anderson-Hafermann et al., 1992; Mian and Garlich et al., 1995), which is a globulin-type protein having a molecular weight of 24,000 and isoelectric point of 4.5 (Kunitz, 1945). Trypsin inhibitor inhibits the conversion of zymogens to active proteases of trypsin and chymotrypsin. The mechanism of action differs for trypsin and chymotrypsin (Kunitz, 1947). Trypsin inhibitor binds with trypsinogen to form an irreversible compound preventing the formation of an active protease. Conversely, trypsin inhibitor action of chymotrypsin is less pronounced forming a reversible dissociated compound (Northrop, 1922).
In addition to its detrimental effects on proteolytic action, trypsin inhibitor dramatically affects the size of the pancreas and amount of trypsinogen produced. Chernick et al. (1948) reported that pancreas weight as a percent of body weight was increased by 56% and had 43% higher trypsinogen content per gram of pancreas nitrogen content with chicks fed diets containing raw soybean meal compared with diets containing heat-treated soybean meal. Moreover, Lyman and Lepkovsky (1957) reported low trypsin content in the small intestine of rats immediately after feeding a diet containing raw soybean meal, but increased 3 fold the normal concentration 6 hours postfeeding. This provides evidence the pancreas produced trypsinogen in excess to compensate for the trypsin inhibitor. Hence, the justification for the trypsin content observed several hours after feeding. The inhibitory action is reduced by subjecting soybeans or soybean meal to heat by deactivating anti-nutritional toxins (Hayward et al., 1936; Kunitz, 1947). Broiler growth has been shown to be increased by approximately 140 to 150% with autoclaving raw hexane-extracted soybeans or soybean meal compared with chicks fed diets containing raw hexane-extracted soybeans or soybean meal not subjected to heat (Araba and Dale, 1990b; Anderson-Hafermann, 1992). If adequate heat is not applied during soybean processing, soybean meal will be produced containing active toxins compromising its nutritional value.
5. Overheating of soybean meal
Overheating of soybean meal reduces its nutritional value for poultry (Renner et al., 1953; Warnick and Anderson, 1968; Araba and Dale, 1990a). It has been shown that overcooking of soybean meal decreases digestibility of amino acids (Lee and Garlich, 1992; Parsons et al., 1992). The explanation for the decreased amino acid digestibility and reduced growth responses appear to be related to the Maillard reaction with cross-linking involved to a lesser extent. Parsons et al. (1992) examined the effects of overprocessing dehulled, solvent-extracted soybean meal by autoclaving at 121◦C and 105 kPa for 0, 20, 40, and 60 min. Increasing the time of autoclaving reduced total concentration of lysine, arginine and cysteine, but other amino acids were not influenced by overprocessing. The largest decrease in true amino acid digestibility occurred with lysine, cystine, histidine, and aspartic acid, whereas digestibility of threonine, serine, alanine, and leucine was decreased to a lesser extent. Moreover, a growth assay using broiler chicks determined that autoclaving at 121◦C for 40 min reduced lysine bioavailability by 15% compared with birds fed soybean meal not subjected to autoclaving. The destruction of lysine and arginine content of soybean meal and reduced lysine digestibility due to autoclaving indicates the presence of the Maillard reaction. In addition to chemical composition, color differences are apparent with soybean meal subjected to overprocessing indicating a browning during the latter stage of Maillard reaction (Figure 2).
Maillard reaction is a series of complex reactions occurring when feed ingredients, food, and animal tissues are subjected to overprocessing (Iqbal et al., 1999; Fayle and Gerrard, 2002). The series of reactions involve early, advanced, and final stages (Mauron, 1981). In the early reactions, amino groups react with aldehyde groups of free sugars producing a schiff base, which cyclizes to form a glycosylamine (Mauron, 1981; Dillis, 1993). The glycosylamine undergoes a rearrangement to form either Amadori products (1-amino-1-deoxy-2-ketose) if produced from glucose or Heyns products if derived from fructose. In this series of reactions, ε-amino group of lysine is affected the most and ε-amino groups located at the terminal end of proteins are also involved but to a lesser extent. With lysine, an aldose is changed to a ketose creating a fructosyl-lysine. In the advanced reactions, Amadori or Heyns products are decomposed to form deoxydicarbonyl sugars and these resulting sugar derivatives can react with other amino acids producing aldehydes, ketones, and/or deoxydicarbonyl compounds (Dillis, 1993). Heterocylic compounds (pyrazines, pyrroles, pyridines, and thiazoles) are formed during the latter stages of these reactions, which are known to provide aromas and flavor to food (Mauron, 1981; Dillis, 1993). In the final reactions, food or feed ingredients are characterized by exhibiting a dark color associated with brown melanoidin pigments produced by this set of reactions, hence the name of browning well known for the Maillard reaction (Hurrell and Carpenter, 1981). Proteins are modified through cross-linking reactions as deoxydicarbonyl sugars or carbonyl compounds react with amino acids (Mauron, 1981; Dillis, 1993).
Poor digestibility of intact protein sources subjected to overprocessing (Maillard reaction) may be due to the formation of Amadori or Heyns products, reduced absorption of lysine, and the formation of cross-links (Mauron, 1981; Sherr et al., 1989; Dillis, 1993). Sherr et al. (1989) determined that, in the presence of Maillard products derived from lysine (glycosylated lysine derivatives), absorption of lysine was inhibited. The glycosylated lysine derivatives compete with lysine for absorption carriers, but the majority of these derivatives have poor utilization with excretion being 72 and 96% of the amounts absorbed. The cross-links are not very digestible as endogenous proteases are not able to cleave this complex during digestion resulting in poor utilization to the animal. Soybean meal contains sugar complexes in the form of raffinose and stachyose and overprocessing may contribute to Maillard reactions (Hancock et al., 1990). Cysteine content has been shown to be reduced in soybean meal with overprocessing (Parsons et al., 1992). Cysteine is not thought to be involved with Maillard reactions, but rather forming lanthionine during overprocessing (Miller et al., 1965; Hurrell et al., 1976). With the formation of lanthionine, cysteine would probably be expected to decrease when soybean meal is subjected to overprocessing.
Figure 2.
Soybean meal samples exposed to varying temperatures with samples on the bottom row subjected to excessive heating as noted by the darker color (Courtesy of Dr. N. Dale, Department of Poultry Science, University of Georgia).
6. Analytical assays to estimate soybean meal quality
Based on the popularity of soybean meal as a protein source in poultry and swine feeds, it is not surprising that quite a lot of time and effort are expended in measuring soybean meal protein quality. Over the years, a number of techniques have been examined to measure the protein quality of plant protein products. Those most used in practice have changed as research-based comparisons of the various techniques have shed light into the relative merits of each. Currently, the analytical technique most commonly used to measure soybean meal quality is protein solubility, perhaps combined with the urease test. Protein solubility has been a tool to test soybean meal solubility for many decades (Smith and Circle, 1938, Lund and Sandstrom, 1943). These early attempts examined protein solubility in water. Later, a range of acid and alkaline chemicals were compared for their utility in measuring soybean meal protein solubility. More recently, Araba and Dale (1990a) and Parsons et al. (1991) examined the use of a 0.2% potassium hydroxide (KOH) solution. Protein (nitrogen) concentration is then quantified using the kjeldahl method. In general, KOH solubility decreases as the degree of heat treatment associated with soybean processing increases. While raw soybean products would be 100% soluble, they obviously have a full complement of antinutritional factors that have not been deactivated. Research comparing protein solubility to other measures of protein quality indicate that KOH solubilities between 78 to 84% are optimal for animal performance. Values ranging from 84 to 89% are slightly under-processed and may be acceptable for older animals, while values under 74% are over-processed and will have reduced lysine digestibility. Araba and Dale (1990b) compared protein solubility to Orange G binding and trypsin inhibitor activity. They found that protein solubility compared favorably to measurements of broiler growth and trypsin inhibitor activity while the Orange G binding technique was not sensitive to processing changes in autoclaved soybean meals (Figure 3). The combined works of Araba and Dale (1990a,b) concluded that the KOH solubility test is useful for detecting both over-processed and under-processed soybean meals.
The urease test has been used for some time as a measure of soybean meal processing. Urease is an enzyme in soybean meal that is of little interest in animal nutrition. It is, however, easier to measure than many of the antinutritional factors of interest. Because trypsin inhibitors and lectins are denatured by heat processing of soybeans at a similar rate to the urease enzyme, testing for urease is a useful marker for degree of soybean meal underprocessing (Caskey and Knapp, 1944; Wright, 1981). Unfortunately, the urease test does not do an adequate job of measuring overprocessed meals. Over time, meals ranging from 0.05 to 0.15 change in pH were considered properly processed for poultry. Recently, meals higher than a 0.15 pH change have been deemed usable by older chickens. Also, changes in soybean processing methods have raised questions regarding the lower range of this test (i.e. levels under 0.05 pH may not cause problems).
Figure 3.
Effects on protein solubility and Orange G binding of overprocessed soybean meal (Araba and Dale, 1990b).
Despite the ease of measuring the urease enzyme as opposed to more complicated assays, it is possible to routinely measure trypsin inhibitors in soybean meals. Directly measuring trypsin inhibitors in soybean meals is obviously a desirable assay and trypsin inhibitors are one of the major antinutritional factors of note. Kakade et al. (1974) described the most commonly-used method for determining trypsin inhibitors in soybean products for animal feeds. Work by Mc Naughton et al. (1981) indicated that direct measurement of trypsin inhibitor levels was an accurate indicator of animal performance for undercooked soybean products. For practical applications, the easier-to-complete urease test still predominates as a marker for under-processed soybean meals.
The use of Orange G dye to determine the amount of heat processing a soybean meal sample has been subjected to is based on the dye’s ability to bind the free ε-amino group of lysine under acidic conditions. As lysine progressively becomes less available during extended heat processing, less of the Orange G dye can bind. Moran et al. (1963) correlated Orange G dye binding with broiler chick growth and found agreement across a range of heat treatments (autoclaving in this case). Araba and Dale (1990b) found protein solubility more sensitive to soybean meal processing variation than the Orange G binding technique.
There are other dye binding tests that have been suggested as methods to monitor soybean meal quality, including the cresol red test (Olomucki and Bornstein, 1960; Vorha and Kratzer, 1991) and coomassie blue staining (Vorha and Kratzer, 1991). A coomassie blue dye solution can be used to titrate protein solubility after KOH treatment in place of the kjeldahl protein test (Kratzer et al., 1990). The optical density of the stained proteins is then measured against a set of lysozyme standards at 595 nm. Coomassie blue staining may be more accurate than the kjeldahl procedure at measuring protein solubility because coomassie blue binds with intact proteins and not free amino acids (Vorha and Kratzer, 1991), also, the coomassie blue dye test would be faster in producing results than using the Kjeldahl portion of the KOH solubility test. Because this is, in essence, a KOH solubility test, it is particularly useful in detecting overprocessed soybean meals.
Protein dispersibility index refers to the amount of soybean meal protein dispersed in water after blending a soybean meal sample in water with a high speed blender. Research by Batal et al. (2000) correlated chick growth with several methods of soybean meal quality assessment in meals that had been heat treated. Their results indicated that protein dispersibility index was a sensitive measure of soybean meal quality and gave better results than either the urease or protein solubility assays. Protein dispersibility indexes of 40 to 45% indicate a soybean meal that is neither over- or under-processed. These authors suggested that the protein dispersibility index will give an accurate picture of soybean processing if paired with another test such as the urease test. A number of other tests have been proposed to measure soybean meal quality, including formaldehyde titration (Almquist and Maurer, 1953) and a fluorescence test (Hsu et al., 1949).
In conclusion, nutritional quality of soybean meal is of utmost importance to optimize the rate and efficiency of growth of poultry. It is necessary for ingredient quality control programs to understand the appropriate assays to determine if soybean meal has been subjected to under- or over-processing (Table 3). Protein solubility assay is easily conducted and provides more reproducible results than trypsin inhibitor activity assay. A value greater than 85% denotes underprocessing, whereas a protein solubility index less than 74% infers overheating. Protein dispersibility index is also a useful tool to measure protein quality with values ranging from 40 to 45% denoting acceptable quality. Conversely, urease activity is useful only for detecting underprocessing because its activity falls to zero as soybean meal has been exposed to overprocessing. Moreover, Orange G binding capacity exhibits small change with soybean meal subjected to overprocessing, hence this assay may not be appropriate to detect overheated soybean meal.
Technique
Underprocessing
Overprocessing
Comments
KOH Solubility
Acceptable Assay
Acceptable Assay
Commonly used
Orange G Binding
Not useful
Very little change
Low sensitivity
Trypsin Inhibitor
Acceptable Assay
Not useful
Complicated, time consuming, and expensive
Urease
Acceptable Assay
Activity falls to zero
Commonly used
Protein dispersibility
Acceptable Assay
Acceptable Assay
Has potential but is not commonly used
Table 3.
Comparison of analytical techniques for under- and over-processed soybean meal
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(Joe) Hess",slug:"joseph-b.-(joe)-hess",email:"hessjos@auburn.edu",position:null,institution:{name:"Auburn University",institutionURL:null,country:{name:"United States of America"}}}],sections:[{id:"sec_1",title:"1. Introduction ",level:"1"},{id:"sec_2",title:"2. Soybean meal in poultry and swine feeds ",level:"1"},{id:"sec_3",title:"3. Protein digestion ",level:"1"},{id:"sec_4",title:"4. Trypsin inhibtor in soybean meal and protein digestion ",level:"1"},{id:"sec_5",title:"5. Overheating of soybean meal",level:"1"},{id:"sec_6",title:"6. Analytical assays to estimate soybean meal quality",level:"1"}],chapterReferences:[{id:"B1",body:'AdedokunS. A.ParsonsC. M.M. S.LilburnO.AdeolaApplegateT. J.2007Comparison of ileal endogenous amino acid flows in broiler chicks and turkey poults.Poult. Sci. 8616821689\n\t\t\t'},{id:"B2",body:'AlpersD. H.1994Digestion and absorption of carbohydrates and proteins. 17231749in Physiology of the Gastrointestinal Tract. L. R. Johnson, D. H. Alpers, J. 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The Soybean Meal Information Center, United Soybean Board. www.soymeal.orgAccessed on March 15, 2011.'},{id:"B62",body:'WaldroupP. W.CottonT. L.1974Maximum usage levels of cooked, full-fat soybeans in all-mash broiler diets. Poult. Sci. 53677680\n\t\t\t'},{id:"B63",body:'WaldroupP. W.SmithK.1999Soybean Use- Poultry. Soybean Meal Information Center Fact Sheet. The Soybean Meal Information Center, United Soybean Boardwww.soymeal.orgAccessed on March 15, 2011.'},{id:"B64",body:'WarnickR. E.AndersonJ. O.1968Limiting essential amino acids in soybean meal for growing chickens and the effects of heat upon availability of the essential amino acids.Poult. Sci. 47281287\n\t\t\t'},{id:"B65",body:'WrightK. N.1981Soybean meal processing and quality controlJ. Am. Oil Chem. Soc. 58296300\n\t\t\t'}],footnotes:[],contributors:[{corresp:"yes",contributorFullName:"W.A. III. Dozier",address:null,affiliation:'
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Moores",authors:[{id:"37445",title:"Dr.",name:"Robin",middleName:null,surname:"Gunning",fullName:"Robin Gunning",slug:"robin-gunning"},{id:"45768",title:"Dr.",name:"Graham",middleName:null,surname:"Moores",fullName:"Graham Moores",slug:"graham-moores"}]},{id:"19746",title:"Conjugated Linoleic Acid: A Milk Fatty Acid with Unique Health Benefit Properties",slug:"conjugated-linoleic-acid-a-milk-fatty-acid-with-unique-health-benefit-properties",signatures:"Kathirvelan Chinnadurai and Amrish Tyagi",authors:[{id:"36882",title:"Dr.",name:"Kathirvelan",middleName:null,surname:"Chinnadurai",fullName:"Kathirvelan Chinnadurai",slug:"kathirvelan-chinnadurai"},{id:"135714",title:"Dr.",name:"Amrish",middleName:null,surname:"Tyagi",fullName:"Amrish Tyagi",slug:"amrish-tyagi"}]},{id:"19747",title:"Lunasin, a Cancer Preventive Seed Peptide",slug:"lunasin-a-cancer-preventive-seed-peptide",signatures:"Blanca Hernández-Ledesma, Chia-Chien Hsieh, Vermont Dia, Elvira González de Mejia and Ben O. de Lumen",authors:[{id:"29648",title:"Prof.",name:"Elvira",middleName:null,surname:"Gonzalez De Mejia",fullName:"Elvira Gonzalez De Mejia",slug:"elvira-gonzalez-de-mejia"},{id:"36395",title:"Prof.",name:"Ben O.",middleName:null,surname:"de Lumen",fullName:"Ben O. de Lumen",slug:"ben-o.-de-lumen"},{id:"36572",title:"Dr.",name:"Blanca",middleName:null,surname:"Hernández-Ledesma",fullName:"Blanca Hernández-Ledesma",slug:"blanca-hernandez-ledesma"},{id:"36573",title:"Dr.",name:"Chia-Chien",middleName:null,surname:"Hsieh",fullName:"Chia-Chien Hsieh",slug:"chia-chien-hsieh"},{id:"92660",title:"Mr.",name:"Vermont",middleName:null,surname:"Dia",fullName:"Vermont Dia",slug:"vermont-dia"}]},{id:"19748",title:"Insights into the Pharmacological Effects of Soy Isoflavones on Catecholamine System",slug:"insights-into-the-pharmacological-effects-of-soy-isoflavones-on-catecholamine-system",signatures:"Nobuyuki Yanagihara, Yumiko Toyohira, Minhui Liu, Susumu Ueno, Masato Tsutsui and Han Zhang",authors:[{id:"33364",title:"Prof.",name:"Nobuyuki",middleName:null,surname:"Yanagihara",fullName:"Nobuyuki Yanagihara",slug:"nobuyuki-yanagihara"},{id:"37854",title:"Dr.",name:"Yumiko",middleName:null,surname:"Toyohira",fullName:"Yumiko Toyohira",slug:"yumiko-toyohira"},{id:"37855",title:"Dr.",name:"Susumu",middleName:null,surname:"Ueno",fullName:"Susumu Ueno",slug:"susumu-ueno"},{id:"37856",title:"Ms.",name:"Han",middleName:null,surname:"Zhang",fullName:"Han Zhang",slug:"han-zhang"},{id:"37857",title:"Prof.",name:"Masato",middleName:null,surname:"Tsutsui",fullName:"Masato Tsutsui",slug:"masato-tsutsui"},{id:"89081",title:"BSc.",name:"Minhui",middleName:null,surname:"Liu",fullName:"Minhui Liu",slug:"minhui-liu"}]},{id:"19749",title:"Occurrence of Biogenic Amines in Soybean Food Products",slug:"occurrence-of-biogenic-amines-in-soybean-food-products",signatures:"Shruti Shukla, Jong-Kyu Kim and Myunghee Kim",authors:[{id:"33323",title:"Prof.",name:"Myunghee",middleName:null,surname:"Kim",fullName:"Myunghee Kim",slug:"myunghee-kim"},{id:"45053",title:"Dr.",name:"Shruti",middleName:null,surname:"Shukla",fullName:"Shruti Shukla",slug:"shruti-shukla"},{id:"45055",title:"Prof.",name:"Jong-Kyu",middleName:null,surname:"Kim",fullName:"Jong-Kyu Kim",slug:"jong-kyu-kim"}]},{id:"19750",title:"Biologically Active Molecules from Soybeans",slug:"biologically-active-molecules-from-soybeans",signatures:"Michio Kurosu",authors:[{id:"33087",title:"Prof.",name:"Michio",middleName:null,surname:"Kurosu",fullName:"Michio Kurosu",slug:"michio-kurosu"}]},{id:"19751",title:"From Soybean Phytosterols to Steroid Hormones",slug:"from-soybean-phytosterols-to-steroid-hormones",signatures:"Feng-Qing Wang, Kang Yao and Dong-Zhi Wei",authors:[{id:"32646",title:"Dr.",name:"Feng-Qing",middleName:null,surname:"Wang",fullName:"Feng-Qing Wang",slug:"feng-qing-wang"},{id:"32662",title:"MSc.",name:"Kang",middleName:null,surname:"Yao",fullName:"Kang Yao",slug:"kang-yao"},{id:"32663",title:"Prof.",name:"Dong-Zhi",middleName:null,surname:"Wei",fullName:"Dong-Zhi Wei",slug:"dong-zhi-wei"}]},{id:"19752",title:"Genistein Derivatization – From a Dietary Supplement to a Pharmaceutical Agent",slug:"genistein-derivatization-from-a-dietary-supplement-to-a-pharmaceutical-agent",signatures:"Aleksandra Rusin and Zdzisław Krawczyk",authors:[{id:"32402",title:"Dr.",name:"Aleksandra",middleName:null,surname:"Rusin",fullName:"Aleksandra Rusin",slug:"aleksandra-rusin"},{id:"47345",title:"Prof.",name:"Zdzislaw",middleName:"Tadeusz",surname:"Krawczyk",fullName:"Zdzislaw Krawczyk",slug:"zdzislaw-krawczyk"}]},{id:"19753",title:"Soybean Oil: Production Process, Benefits and Uses in Pharmaceutical Dosage Form",slug:"soybean-oil-production-process-benefits-and-uses-in-pharmaceutical-dosage-form",signatures:"H. Yesim Karasulu, Ercüment Karasulu, Mevlüt Büyükhelvacıgil, Mustafa Yıldız, Ahmet Ertugrul, Kadir Büyükhelvacıgil, Zeliha Ustün and Nilay Gazel",authors:[{id:"32324",title:"Dr.",name:"H.Yesim",middleName:null,surname:"Karasulu",fullName:"H.Yesim Karasulu",slug:"h.yesim-karasulu"},{id:"82745",title:"Dr.",name:"Ercument",middleName:null,surname:"Karasulu",fullName:"Ercument Karasulu",slug:"ercument-karasulu"},{id:"83589",title:"Dr.",name:"Mevlut",middleName:null,surname:"Buyukhelvacigil",fullName:"Mevlut Buyukhelvacigil",slug:"mevlut-buyukhelvacigil"},{id:"83590",title:"BSc.",name:"Mustafa",middleName:null,surname:"Yildiz",fullName:"Mustafa Yildiz",slug:"mustafa-yildiz"},{id:"83591",title:"MSc.",name:"Ahmet",middleName:null,surname:"Ertugrul",fullName:"Ahmet Ertugrul",slug:"ahmet-ertugrul"},{id:"83592",title:"MSc.",name:"Kadir",middleName:null,surname:"Buyukhelvacigil",fullName:"Kadir Buyukhelvacigil",slug:"kadir-buyukhelvacigil"},{id:"83593",title:"MSc.",name:"Zeliha",middleName:null,surname:"Ustun",fullName:"Zeliha Ustun",slug:"zeliha-ustun"},{id:"83607",title:"MSc",name:"Nilay",middleName:null,surname:"Gazel",fullName:"Nilay Gazel",slug:"nilay-gazel"}]},{id:"19754",title:"Beneficial Effects of Bioactive Peptides Derived from Soybean on Human Health and Their Production by Genetic Engineering",slug:"beneficial-effects-of-bioactive-peptides-derived-from-soybean-on-human-health-and-their-production-b",signatures:"Chin Feng Liu and Tzu Ming Pan",authors:[{id:"32209",title:"Prof.",name:"Tzu-Ming",middleName:null,surname:"Pan",fullName:"Tzu-Ming Pan",slug:"tzu-ming-pan"},{id:"45625",title:"Ph.D.",name:"Chin-Feng",middleName:null,surname:"Liu",fullName:"Chin-Feng Liu",slug:"chin-feng-liu"}]},{id:"19755",title:"Soy Isoflavones as Bioactive Ingredients of Functional Foods",slug:"soy-isoflavones-as-bioactive-ingredients-of-functional-foods",signatures:"Lutz Mariane",authors:[{id:"30301",title:"Prof.",name:"Mariane",middleName:null,surname:"Lutz",fullName:"Mariane Lutz",slug:"mariane-lutz"}]},{id:"19756",title:"Soybean Oil: How Good or How Bad in Comparison with Other Dietary Oils in the Context of Colon Cancer",slug:"soybean-oil-how-good-or-how-bad-in-comparison-with-other-dietary-oils-in-the-context-of-colon-cancer",signatures:"Tatiana Fiche Salles Teixeira, Ana Paula Boroni Moreira, Damiana Diniz Rosa and Maria do Carmo Gouveia Peluzio",authors:[{id:"30193",title:"Dr.",name:"Maria Do Carmo",middleName:"Gouveia",surname:"Peluzio",fullName:"Maria Do Carmo Peluzio",slug:"maria-do-carmo-peluzio"},{id:"47516",title:"MSc",name:"Damiana",middleName:"Diniz",surname:"Diniz Rosa",fullName:"Damiana Diniz Rosa",slug:"damiana-diniz-rosa"},{id:"47517",title:"MSc",name:"Ana Paula",middleName:null,surname:"Boroni Moreira",fullName:"Ana Paula Boroni Moreira",slug:"ana-paula-boroni-moreira"},{id:"47518",title:"Ms",name:"Tatiana",middleName:null,surname:"Fiche Sales Teixeira",fullName:"Tatiana Fiche Sales Teixeira",slug:"tatiana-fiche-sales-teixeira"}]},{id:"19757",title:"Anti-Diarrhoeal Aspects of Fermented Soya Beans",slug:"anti-diarrhoeal-aspects-of-fermented-soya-beans",signatures:"P.J. Roubos-van den Hil and M.J.R. Nout",authors:[{id:"30073",title:"Dr.",name:"Petra",middleName:null,surname:"Roubos-Van Den Hil",fullName:"Petra Roubos-Van Den Hil",slug:"petra-roubos-van-den-hil"},{id:"46996",title:"Dr.",name:"M.J.",middleName:"Rob",surname:"Nout",fullName:"M.J. Nout",slug:"m.j.-nout"}]},{id:"19758",title:"Antioxidant and Hypocholesterolemic Effects of Soy Foods and Cardiovascular Disease",slug:"antioxidant-and-hypocholesterolemic-effects-of-soy-foods-and-cardiovascular-disease",signatures:"Eugene A. Borodin, Iraida G. Menshikova, Vladimir A. Dorovskikh, Natalya A. Feoktistova, Mikhail A. Shtarberg, Tatyana V. Aksenova, Takashi Yamamoto, Kiyoharu Takamatsu, Hiroyuki Mori and Shigeru Yamamoto",authors:[{id:"29853",title:"Prof.",name:"Eugene",middleName:null,surname:"Borodin",fullName:"Eugene Borodin",slug:"eugene-borodin"},{id:"44009",title:"Prof.",name:"Iraida",middleName:null,surname:"Menshikova",fullName:"Iraida Menshikova",slug:"iraida-menshikova"},{id:"44010",title:"Prof.",name:"Vladimir",middleName:null,surname:"Dorovskikh",fullName:"Vladimir Dorovskikh",slug:"vladimir-dorovskikh"},{id:"44011",title:"Prof.",name:"Natalya",middleName:null,surname:"Feoktistova",fullName:"Natalya Feoktistova",slug:"natalya-feoktistova"},{id:"44012",title:"Prof.",name:"Mikhail",middleName:null,surname:"Shtarberg",fullName:"Mikhail Shtarberg",slug:"mikhail-shtarberg"},{id:"44013",title:"Prof.",name:"Tatyana Aksenova",middleName:null,surname:"Aksenova",fullName:"Tatyana Aksenova Aksenova",slug:"tatyana-aksenova-aksenova"},{id:"44014",title:"Prof.",name:"Takashi",middleName:null,surname:"Yamamoto",fullName:"Takashi Yamamoto",slug:"takashi-yamamoto"},{id:"44015",title:"Prof.",name:"Kiyoharu",middleName:null,surname:"Takamatsu",fullName:"Kiyoharu Takamatsu",slug:"kiyoharu-takamatsu"},{id:"44016",title:"Prof.",name:"Hiroyuki",middleName:null,surname:"Mori",fullName:"Hiroyuki Mori",slug:"hiroyuki-mori"},{id:"44017",title:"Prof.",name:"Shigeru",middleName:null,surname:"Yamamoto",fullName:"Shigeru Yamamoto",slug:"shigeru-yamamoto"}]},{id:"19759",title:"Important Minor Soybens Proteins: Soybean Allergens and Enzymes Inhibitors",slug:"important-minor-soybens-proteins-soybean-allergens-and-enzymes-inhibitors",signatures:"Lenka Vorlova",authors:[{id:"29875",title:"Prof.",name:"Lenka",middleName:"-",surname:"Vorlová",fullName:"Lenka Vorlová",slug:"lenka-vorlova"}]},{id:"19760",title:"Soybean Allergens: Presence, Detection and Methods for Mitigation",slug:"soybean-allergens-presence-detection-and-methods-for-mitigation",signatures:"Weihua Wade Yang, Elvira Gonzalez de Mejia, Huanyu Zheng and Youngsoo Lee",authors:[{id:"29648",title:"Prof.",name:"Elvira",middleName:null,surname:"Gonzalez De Mejia",fullName:"Elvira Gonzalez De Mejia",slug:"elvira-gonzalez-de-mejia"},{id:"29643",title:"Dr.",name:"Weihua Wade",middleName:null,surname:"Yang",fullName:"Weihua Wade Yang",slug:"weihua-wade-yang"},{id:"102733",title:"Dr.",name:"Huanyu",middleName:null,surname:"Zheng",fullName:"Huanyu Zheng",slug:"huanyu-zheng"},{id:"102734",title:"Dr.",name:"Youngsoo",middleName:null,surname:"Lee",fullName:"Youngsoo Lee",slug:"youngsoo-lee"}]},{id:"19761",title:"Nutritional and Bioactive Compounds of Soybean: Benefits on Human Health",slug:"nutritional-and-bioactive-compounds-of-soybean-benefits-on-human-health",signatures:"Hércia Stampini Duarte Martino, Leandro de Morais Cardoso, Sônia Machado Rocha Ribeiro, Maria Inês de Souza Dantas, Newton Deniz Piovesan and Elvira De Mejía",authors:[{id:"28753",title:"Dr.",name:"Hércia Stampini",middleName:null,surname:"Duarte Martino",fullName:"Hércia Stampini Duarte Martino",slug:"hercia-stampini-duarte-martino"},{id:"47475",title:"Dr.",name:"Maria Inês",middleName:null,surname:"Dantas",fullName:"Maria Inês Dantas",slug:"maria-ines-dantas"},{id:"47476",title:"Prof.",name:"Sonia",middleName:null,surname:"Ribeiro",fullName:"Sonia Ribeiro",slug:"sonia-ribeiro"},{id:"47478",title:"MSc.",name:"Glaucia",middleName:null,surname:"Andrade",fullName:"Glaucia Andrade",slug:"glaucia-andrade"}]},{id:"19762",title:"Polyamines - The Principal Candidate Substance of Soybean-Induced Health",slug:"polyamines-the-principal-candidate-substance-of-soybean-induced-health",signatures:"Kuniyasu Soda",authors:[{id:"29223",title:"Prof.",name:"Kuniyasu",middleName:null,surname:"Soda",fullName:"Kuniyasu Soda",slug:"kuniyasu-soda"}]}]}]},onlineFirst:{chapter:{type:"chapter",id:"70551",title:"Relationship of Parasitic Index and Cytokine Profile in Canine Visceral Leishmaniasis",doi:"10.5772/intechopen.90573",slug:"relationship-of-parasitic-index-and-cytokine-profile-in-canine-visceral-leishmaniasis",body:'\n
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1. Introduction
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Visceral leishmaniasis (VL) is a parasitic zoonotic disease caused by the protozoan Leishmania infantum (syn. L. chagasi), an intracellular parasite of the phagocytic mononuclear system [1, 2]. In Brazil, VL is transmitted by sandflies, Lutzomyia longipalpis [1, 3, 4].
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In a global scenario, it is estimated that 300,000 new cases of VL occur with a rate of 20,000 deaths each year, with 94% new cases reported in Brazil, Ethiopia, India, Kenya, Somalia, South Sudan, and Sudan [5]. While in Latin America, LV spreads from Mexico to Argentina, with the largest number of cases concentrated in Brazil [6]. With the urbanization of VL in Brazil, annually, the country records approximately 3500 new cases, mainly in medium and large cities; probably, it is due to the disordered anthropic occupation of the geographic space [7]. Despite scientific advances, cases of VL are expanding, which has a major impact on public health, as dogs are the main reservoirs in the urban environment and therefore play an important role in the transmission cycle [8, 9].
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Canine visceral leishmaniasis (CVL) is characterized by a broad clinical spectrum, from mild and moderate to fatal clinical manifestations. Major clinical signs in dogs include hepatosplenomegaly, lymphadenopathy, exfoliative dermatitis, alopecia, onychogryphosis, keratoconjunctivitis, apathy, anorexia, and severe weight loss [10, 11, 12, 13].
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The clinical manifestation of CVL depends on the interaction of the parasite with the host immune response [2]. In susceptible dogs, clinicopathological abnormalities are preceded by an evident humoral response and depression of the cellular response, mediated by a non-protective Th2 immune response associated with cytokines IL-4, IL-5, IL-6, and IL-10 [14, 15]. Dogs that do not develop the disease have a protective cellular response (Th1) [16, 17], related to INF-γ, TNF-α, IL-2, and IL-12 cytokines.
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Different procedures are used for the diagnosis of CVL [18]. The Brazilian Ministry of Health recommends serology in the investigation of canine disease by the Dual-Path Platform (DPP®) rapid method as a screening test and ELISA as confirmatory test [19]. Other tests are used to demonstrate infection, such as cytology, histopathology [20], and real-time PCR (RT-PCR) [21].
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Similarly, determination of parasitic index has become important for early detection, but also evaluation of treatment efficacy and monitoring of relapses [22]. Thus, the aim of this study was to associate parasitic index to serum cytokine concentration in dogs naturally infected by L. infantum at different clinical stages of infection.
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2. Methodological aspects
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The procedures were previously approved by the Ethics Committee on the Use of Animals (ECUA)/UFMT, Brazil (n° 23108.019567/14-1), and collection of clinical samples was authorized by the dog owners by signing the informed consent form.
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2.1 Animals
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This study was conducted over a 16-month period, evaluating 42 male and female dogs of different ages and breeds from Barra do Garças, Mato Grosso State, Brazil (latitude, −15.893; longitude, 52.2599; south,15° 53′ 35″; west 52° 15′ 36″). Dogs with canine visceral leishmaniasis (n = 21) were classified into clinical stages at diagnosis as described by Solano et al. [23] and confirmed using the Dual-Path Platform Rapid Test (RT DPP®) and polymerase chain reaction (PCR). A control group (n = 21) was also formed, comprising dogs with no clinical changes and negative results for RT DPP® and conventional PCR.
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2.2 Blood and bone marrow sample
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Blood samples (5 mL) were collected by cephalic or jugular venipuncture, placed in tubes without anticoagulant to obtain serum. Serum was obtained by centrifuging the blood sample at 300× g for 5 minutes and was then transferred to 2 mL microtubes and stored at −80°C for cytokine dosing.
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After dog restraint and local anesthesia with 2% lidocaine, bone marrow samples were obtained from the sternal manubrium, placed in microtubes with 0.5 mL 0.9% sterile NaCl solution, and stored at −20°C for subsequent molecular techniques.
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2.3 Immunochromatographic rapid test: RT DPP® kit
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The immunochromatographic rapid test for detection of anti-Leishmania infantum antibodies (DPP®—Canine Visceral Leishmaniasis-Bio-Manguinhos/FIOCRUZ, Rio de Janeiro, Brazil) that uses the recombinant protein K39 (rK39) as an antigen, a cloned 39 amino acid sequence of the specific L. infantum kinase region, was performed according to the manufacturer’s guidance.
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2.4 DNA extraction, conventional PCR, and qPCR
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DNA extraction from blood samples was performed by the phenol-chloroform method. The polymerase chain reaction assay was performed using the primers RV1 (sense) 5′-CTT TTC TGG TCC CGC GGG TAG G-3′ and RV2 (antisense) 5′-CCA CCT GGC TAT TTT ACA CCA-3′ [24], which amplifies the DNA fragment of a 145 bp region of conserved kDNA present in L. infantum. Amplification used 200 mM dNTP, 1 pM from each primer, a buffer solution (10 mM Tris–HCl and 50 mM KCl, pH 8.3), 2 mM MgCl2, 1.5 U Taq DNA polymerase, and 2 μl of the DNA sample in the final volume of 25 μl. Assays were performed for one cycle at 94°C for 4 minutes, followed by 30 cycles at 94°C for 30 seconds, 60°C for 30 seconds, and 72°C for 30 seconds, and final extension of one cycle at 72°C for 10 minutes. The amplification product was fractionated by 2.0% agarose gel electrophoresis, stained with red gel spot, and visualized on a transilluminator (UV, 300 nm).
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Quantitative PCR (qPCR) was performed in triplicate using the StepOne™ Real-Time PCR System Sequence Detection System (Applied Biosystems) targeting RV1–5′-CTT TTC TGG TCC GGG TAG G-3′ primers and RV2–5′-CCA CCT GGC TAT TTT ACA CCA-3′ amplifying a 145 bp sequence of L. infantum-specific kDNA [24]. Reactions were prepared in a 25 μl final volume containing SYBR Green Master Mix, 0.3 μM of each primer, and 2 μl of target DNA. Amplification conditions included an initial incubation step at 94°C for 10 minutes, followed by 40 cycles of amplification, 94°C for 15 seconds, and 60°C for 60 seconds. The standard curve was established for each assay using known amounts of TOPO PCR 2.1 plasmid (Invitrogen Corp.) containing L. infantum kDNA gene. Serial (10×) dilutions of the recombinant plasmid containing 2.9×104–2.9×108 copies of the plasmid were performed and used on the standard curve.
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2.5 Cytokine quantification by flow cytometry
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Serum cytokine concentration (IL-2, IL-4, IL-6, IL-10, TNF-α, IFN-γ, and IL-17) was assessed using the Cytometric Bead Array (CBA) Kit (BD Bioscience, USA) and evaluated by a flow cytometer (FACSCalibur®, BD Bioscience, USA). The reading was done using the CellQuest. Data were analyzed in FCAP array software version 5.0.
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2.6 Determination of serum immunoglobulins
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Immunoglobulin concentrations (IgM and IgG) in the sera were determined by turbidimetric method. For 1:11 (v/v) IgM and 1:15 (v/v) IgG, antibody concentrations were determined using IgM (Bioclin®, Brazil, Ref K063) and IgG (Bioclin®, Brazil, Ref K062) antiserum diluted with 1:12 (v/v). The calibration curve obtained from the Multical calibrator (Bioclin®, Brazil, Ref K064) was used to determine the standard curve for each immunoglobulin. Positive and negative serum samples, standards, and controls were placed in 500 μl buffer solution (0.15 mol/L sodium chloride, Tris 50 mmol/L, 6.0000 PEG 50 g/L, and sodium azide 15.38 nmol/L). The suspensions were mixed and incubated at 37°C for 10 minutes. Reactions were read on a spectrophotometer at 340 nm.
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2.7 Statistical analysis
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For the analysis of the concentration of cytokines and immunoglobulins (IgG and IgM), the Student t-test independent samples were used. For the quantification of parasitic index of the bone marrow and cytokines when compared by clinical stage, Kruskal-Wallis analysis of variance was used. Parasite load correlation analysis of IgG in the presence of cytokines was also performed by calculating the Spearman correlation coefficient. Data were expressed as mean ± standard error. Values less than 0.05 (p < 0.05) were considered significant.
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3. Results
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Most of the 21 dogs in the control group were mongrel dog (15/71%), Labrador retriever (1/5%), dachshund (1/5%), pinscher (3/14%), and rottweiler (1/5%). Age ranged from 14 months to 8 years (average 3.4 years). Thirteen dogs were female (13/62%) and eight dogs were male (8/38%). Most of the 21 dogs with leishmaniasis were dogs from mongrel dog (12/57%), Labrador retriever (1/05%), American pit bull (1/05%), poodle (1/05%), and shih tzu (6/28%). Age ranged from 12 months to 11 years (mean 4.3 years). Six dogs were female (6/29%) and 15 dogs were male (15/72%).
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At the time of clinical evaluation, all dogs diagnosed with VL had several clinicopathological findings typical of the disease. Clinical symptoms in seropositive animals (CVL) included lymphadenopathy (17/13%), skin ulcers (12/10%), onychogryphosis (11/09%), ear ulceration (11/09%), scaling (10/08%), weight loss (9/07%), dermatopathy (8/06%), ophthalmopathy (8/06%), muscle atrophy (4/03%), splenomegaly (7/06%), alopecia (6/05%), lethargy (5/04%), periocular alopecia (4/03%), skin nodules (3/02%), hepatomegaly (3/02%), cachexia (3/02%), and hyperkeratosis (2/01%).
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Dogs were classified into three clinical stages: stage I, mild disease (n = 5/24%); stage II, moderate disease (n = 9/43%); and stage III, severe disease (n = 7/33%). Stage II dogs were not subclassified.
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\nLeishmania infantum DNA was detected in all dogs of the group with CVL up to a concentration of 1 fg/μl. Real-time PCR of bone marrow samples was positive in all dogs in the CVL group (100%). There was no statistical difference in the distribution between clinical stages and parasitic index, as shown in Table 1.
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Cytokines/parasitemia
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I
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II
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III
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p-Value
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IL-2
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6.62 ± 1.18
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12.01 ± 7.99
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15.09 ± 6.34
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0.152
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IL-4
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10.50 ± 2.05
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11.38 ± 3.81
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9.90 ± 2.73
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0.9044
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IL-6
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2.14 ± 0.57
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2.72 ± 0.66
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3.12 ± 0.50
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0.0350
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IL-10
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2.47 ± 0.97
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2.85 ± 0.96
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2.39 ± 0.84
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0.8973
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IL-17
\n
2.22 ± 0.22
\n
12.38 ± 9.63
\n
13.27 ± 7.51
\n
0.4345
\n
\n
\n
TNF-α
\n
4.52 ± 2.12
\n
4.65 ± 2.31
\n
6.14 ± 1.43
\n
0.0462
\n
\n
\n
IFN
\n
3.07 ± 0.99
\n
28.19 ± 23.21
\n
2.58 ± 0.28
\n
0.4648
\n
\n
\n
Parasite copy number (×107)/ml
\n
4.96 ± 1.00
\n
4.63 ± 1.37
\n
4.55 ± 1.49
\n
0.9467
\n
\n\n
Table 1.
Cytokine concentrations and parasite copy number (×107)/ml in dogs with visceral leishmaniasis in different clinical staging.
The results were expressed in mean and standard error.
\n
The mean and standard error of concentrations (pg/ml) of IL-2, IL-4, IL-6, IL-10, TNF-α, IFN-γ, and IL-17 cytokines based on clinical staging in CVL-infected dogs are shown in Table 1. It was observed that IL-6 and TNF-α concentrations increased in serum of infected dogs with significant statistical difference between the clinical stages of CVL, although most infected dogs had moderate and severe clinical manifestations of the disease.
\n
Among dogs with CVL and uninfected dogs, an increase of IL-4 and TNF-α concentrations in serum from dogs infected with CVL was observed. Similar serum concentrations of IL-2, IL-10, IL-17, and IFN-γ were observed between the groups studied (Table 2).
\n
\n
\n
\n
\n
\n\n
\n
Cytokines
\n
Control
\n
CVL
\n
p-Value
\n
\n\n\n
\n
IL-2
\n
9.18 ± 6.14
\n
11.75 ± 6.89
\n
0.3199
\n
\n
\n
IL-4
\n
7.43 ± 2.50
\n
12.56 ± 5.37
\n
0.0469
\n
\n
\n
IL-6
\n
2.87 ± 0.95
\n
2.71 ± 0.67
\n
0.3326
\n
\n
\n
IL-10
\n
2.98 ± 1.39
\n
2.62 ± 0.87
\n
0.2807
\n
\n
\n
IL-17
\n
11.12 ± 12.12
\n
11.63 ± 9.66
\n
0.4570
\n
\n
\n
TNF-α
\n
2.80 ± 0.52
\n
5.12 ± 2.33
\n
0.0009
\n
\n
\n
IFN
\n
13.26 ± 16.88
\n
16.15 ± 19.01
\n
0.3589
\n
\n\n
Table 2.
Cytokine concentrations in dogs noninfected and dogs with canine visceral leishmaniasis.
The results were expressed in mean and standard error.
\n
When comparing immunoglobulin means, IgG levels were elevated in the CVL group when compared to IgM levels. A significant difference (p = <0.0001) was observed. Similarly, IgG concentration between the control and CVL groups was evaluated. IgG levels were found to be higher in serum from dogs with CVL (2300.75 ± 678.463) when compared to control group IgG concentrations (636.94 ± 312.8 mg/dl), showing a significant difference between groups (p = <0.0001). Regarding the comparison of IgM concentration (mg/dl) in the CVL group (279.74 ± 37.755) compared to the control group (241.12 ± 59.835), there was no difference (Table 3).
\n
\n
\n
\n
\n
\n\n
\n
Group
\n
Control
\n
CVL
\n
p-Value
\n
\n\n\n
\n
IgG
\n
636.94 ± 255.52
\n
2288.04 ± 610.08
\n
<0.0001
\n
\n
\n
IgM
\n
241.12 ± 51.81
\n
282.42 ± 33.99
\n
0.0773
\n
\n\n
Table 3.
Immunoglobulin concentrations (IgG and IgM) in serum from dogs with canine visceral leishmaniasis.
The results were expressed in mean and standard error.
\n
Correlations of IL-6 and TNF-α concentrations were analyzed according to clinical staging with parasitic index according to stage I, IL-6 (rs = 0.400, p = 0.5046) and TNF-α (rs = 0.700, p = 0.1881); stage II, IL-6 (rs = 0.7000, p = 0.1881) and TNF-α (rs = −0.1590, p = 0.6828); and stage III, IL-6 (rs = −0.3571, p = 0.4316) and TNF-α (rs = −0.4643, p = 0.2939). There was no correlation between the other parameters evaluated.
\n
The correlation between the parasitic index of dogs with CVL in the presence of cytokine IL-4 and TNF-α in the blood of dogs infected with CVL presented the IL-4 (rs = 0.0240, p = 0.9176) and TNF-α (rs = 0.0825, p = 0.7221). No additional significant correlations were found. Antibody levels were positively correlated with IL-4 expression (rs = 0.5997, p = 0.0040) (Table 4).
\n
\n
\n
\n
\n\n
\n
\n
IgG
\n
\n
\n
\n
Parameters
\n
rs
\n
p-Value
\n
\n\n\n
\n
IL-4
\n
0.5997
\n
0.0040
\n
\n
\n
TNF-α
\n
0.4164
\n
0.0603
\n
\n
\n
Parasitic index
\n
−0.2243
\n
0.3282
\n
\n\n
Table 4.
Correlation between IgG concentrations with IL-4 and TNF-α and parasitic index of dogs infected with CVL.
rs, correlation coefficient of Spearman.
\n
In this study, as shown in Table 5, the correlation of the evolution of clinical signs between the stages presented below was analyzed. There was a significant positive correlation of IL-6 cytokine levels between stage I and stage III.
\n
\n
\n
\n
\n
\n
\n
\n
\n\n
\n
Stage
\n
I and II
\n
I and III
\n
II and III
\n
\n
\n
\n
rs
\n
p
\n
rs
\n
p
\n
rs
\n
p
\n
\n\n\n
\n
IL-6
\n
0.6031
\n
0.0855
\n
0.8469
\n
0.0162
\n
0.5630
\n
0.1144
\n
\n
\n
TNF-α
\n
0.0350
\n
0.9288
\n
0.3784
\n
0.4026
\n
0.0168
\n
0.9658
\n
\n\n
Table 5.
Correlation of IL-6 and TNF-α cytokine levels of dogs with canine visceral leishmaniasis by clinical staging of serum from dogs of the CVL group.
rs, correlation coefficient of Spearman.
\n
\n
\n
4. Discussion
\n
In this study the most dogs in the control group and CVL were mixed breed. The clinical symptoms of seropositive dogs (CVL) included lymphadenopathy, skin ulcers, onychogryphosis, ear ulceration, scaling, weight loss, and others. Dogs were classified into three clinical stages: stage I, mild disease; stage II, moderate disease; and stage III, severe disease. There was no statistical difference in the distribution between clinical stages and parasitic index. IL-6 and TNF-α concentrations increased in serum from infected dogs with a statistically significant difference between the clinical stages of CVL. Between the dogs with CVL and the control group, there was a statistical difference in the serum concentrations of cytokines IL-4 and TNF-α. IgG levels were elevated in the CVL group when compared to IgM levels. Antibody levels were positively correlated with IL-4 expression (rs = 0.5997; p = 0.0040). There was a significant positive correlation of IL-6 cytokine levels between stage I and stage III.
\n
The clinical signs of CVL are important for the diagnosis. In the present study, the most prevalent clinical signs were lymphadenopathy, skin ulcers, onychogryphosis, ear ulceration, and scaling. However, prevalence is highly variable across studies, but generally these clinical signs are the most commonly reported in the literature. These results corroborate the findings of several authors [25, 26].
\n
Regarding gender, there was a greater predominance of males in infected dogs and females in dogs in the control group. Regarding age, it did not present large variations. This fact seems to be associated with the higher risk of male exposure. However, the study shows no statistically significant differences for age and gender between healthy and sick dogs [27].
\n
Bone marrow samples were taken from 21 dogs serologically positive for L. infantum. According to the clinical signs, dogs were classified as stages I, II, and III. Real-time PCR detected no parasite copies (×1010)/μl L. infantum DNA in all animals of the CVL group, distributed as follows: stage I mean (4.964), stage II average (4.63), and stage III (4.55). No statistically significant difference was found in the average amount of DNA copy number between the different clinical stages (p = 0.9467). In bone marrow samples from dogs that are cytologically positive, a high parasitic index is detected [21].
\n
Previous studies report that quantitative PCR on bone marrow samples from positive dogs in conventional tests contained a higher number of Leishmania kDNA copies than peripheral blood, although no significant differences were detected between symptomatic and asymptomatic dogs in terms of parasite load [28]. This literary quote converges with the findings of this study.
\n
PCR can be used for detection of Leishmania in naturally infected dog samples, and PCR-RFLP (restriction fragment length polymorphism) is sensitive for identification of Leishmania species [28]. In addition, qPCR is effective in quantifying Leishmania DNA loading in clinical samples [29]. The blood sample from dogs infected by L. infantum was found by real-time PCR to have a sensitivity of 100% and specificity of 96.4% [30].
\n
Most cytokines remain partially conserved between species; in this sense, the amino acid sequence of humans and canine cytokines shows 49–96% homology, suggesting a high probability of cross-reactivity between monoclonal antibodies; thus antibodies against human cytokines may be recommended as immunological biomarkers under pathological conditions by flow cytometry in human [31] and dogs [32] as used in this study.
\n
In the present work, the serum concentration of cytokines (IL-2, IL-4, IL-6, IL-10, TNF-α, IFN-γ, and IL-17) was compared between the control groups and the group with CVL. In addition, cytokine levels were compared within the CVL group with clinical staging I, II, and III. When comparing the groups, IL-4 and TNF-α were higher in infected dogs than in the control group, showing significant difference between IL-4 (p = 0.0469) and TNF-α (p = 0.0009) groups. In the group with CVL there were differences between stages I and III with significant differences only for cytokines IL-6 (p = 0.0350) and TNF-α (p = 0.0462).
\n
Elevated levels of IL-6 were found in serum from dogs with active leishmaniasis compared to healthy dogs [33]. These results corroborate the findings of this study. However, other authors reported that IL-6 production did not vary significantly between the groups studied [34]. On the other hand were described in the literature that elevated levels of IL-6 in dogs without clinical signs or symptoms in CVL dogs [35], and also highlights that, among other factors, it may indicate a balance between the parasite elimination effort and the active disease. Increased IL-6 levels suggest a restricted ability to control infection [36]. Even in the absence of clinical signs or symptoms, the animals showed granulomas on histopathological evaluation, suggesting chronicity and therefore a longtime course of infection [35]. Innate immune effector cells primarily neutrophils, monocytes, and macrophages produce and respond to IL-6, which may result in amplification of inflammation and a change from an acute inflammatory state to a chronic state [37].
\n
IL-6 expression increases in dogs with active visceral leishmaniasis and may be a useful marker for active disease [33, 35]. Increased IL-6 production is not directly related to anti-Leishmania antibody titers, suggesting that other cytokines may be involved with hypergammaglobulinemia [33].
\n
As shown in this work, it was observed that there was correlation of IL-6 expression between stages I and III of bone marrow aspirate of dogs infected with CVL. IL-6 production in dogs with active leishmaniasis appears to be associated with severe disease [33]. This statement converges with the findings in this study, as the dogs used in the control group were mostly stage II and III. IL-6 is essential for terminal B-cell differentiation and immunoglobulin production [38].
\n
TNF-α concentration was higher in infected dogs than in the control group, as detected by de Lima et al. [33]. CVL susceptibility is closely associated with downregulation of key cytokines such as IFN-γ, TNF-α, and IL-17A, thus impairing iNOS activation and NO production and favoring parasite replication and disease development [39].
\n
The increased activity of TNF-α in the liver of infected dogs compared to healthy canines has been reported [37, 40]. Higher TNF-α levels in infected dogs indicate that the presence of L. infantum induces an immune response with relevant TNF-α expression when the protozoan is present [40].
\n
Studies suggest that decreased survival of L. infantum in canine macrophages is associated with increased TNF-α and IFN-γ production and decreased IL-10 production [41].
\n
In dogs naturally infected with L. infantum, increased hepatic TNF-α may be associated with increased parasite load on this organ [42]. The cytokines IL-2, IL-4, IL-10, IFN-γ, TNF-α, and IL-12 may be used as markers in epidemiological studies conducted in endemic areas to distinguish between different clinical forms of VL [15]. However, Lima et al. [33] indicate that TNF-α is not considered a good marker of active disease in dogs with VL.
\n
A study has reported a significant relationship between bone marrow IL-4 detection in naturally infected dogs with and without clinical signs and disease severity, suggesting that IL-4 production is associated with pathology [43]. Increased expression of IL-4 cytokine is associated with both severe clinical signs and a high parasitic index on skin lesions [44]. In bone marrow aspirates, IL-4 was elevated in naturally infected dogs with more severe symptoms [43].
\n
The study points to evidence that IL-4 cytokine polymorphism may contribute to innate immunity to L. infantum infection [45].
\n
Antibody levels were positively correlated with IL-4 expression (rs = 0.5997; p = 0.0040). IgG is also linked to chronic infection in patients with VL, where high levels of IgG are predictive of the disease. This finding is in line with the study by Lima et al. [33] suggesting that other cytokines, such as IL-10 or IL-4, may be associated with hypergammaglobulinemia observed in dogs with CVL. Previous studies have detected increased serum IgG levels in symptomatic dogs compared with healthy dogs and are related to pathophysiological disorders and active disease [33].
\n
Response to natural infection of L. infantum is linked to the presence of IgG [43] and Leishmania-specific IgM antibodies that can be detected in infected dogs [46]. Some studies have reported that increased total protein is frequent in dogs infected with visceral leishmaniasis due to increased antibody production [47, 48].
\n
\n
\n
5. Conclusion
\n
These results may contribute to a better understanding of the immune response in dogs infected with L. infantum. Antibody levels were positively correlated with IL-4 expression. There was a significant positive correlation of IL-6 cytokine levels with the evolution of stages I and III. However, this cytokine can be used as a marker to distinguish between different clinical stages.
\n
\n
Acknowledgments
\n
This research received grants from the Mato Grosso Research Support Foundation (FAPEMAT No. 299032/2010) and from the National Council for Scientific and Technological Development (CNPq No. 447218/2014–0 and No. 305725/2018–1), in Brazil.
\n
Conflict of interest
The authors declare that there is no conflict of interest and nonfinancial competitors.
\n',keywords:"Leishmania infantum, dogs, cytokines, parasitic index, cytometry",chapterPDFUrl:"https://cdn.intechopen.com/pdfs/70551.pdf",chapterXML:"https://mts.intechopen.com/source/xml/70551.xml",downloadPdfUrl:"/chapter/pdf-download/70551",previewPdfUrl:"/chapter/pdf-preview/70551",totalDownloads:187,totalViews:0,totalCrossrefCites:0,dateSubmitted:"September 5th 2019",dateReviewed:"November 20th 2019",datePrePublished:"December 20th 2019",datePublished:"June 17th 2020",dateFinished:null,readingETA:"0",abstract:"Visceral leishmaniasis (VL) is a zoonotic parasitic disease caused by Leishmania infantum (L. chagasi) that infects cells of the monocyte-phagocyte system. This work aims to describe the bone marrow parasitism in dogs naturally infected by L. chagasi, and to correlate with serum concentrations of cytokines and antibody level. It evaluated 42 dogs, 21 uninfected and 21 infected by L. infantum, of both sexes and of different ages; dogs were classified into three clinical stages: stage I, mild disease; stage II, moderate disease; and stage III, severe disease. Parasitic index was determined by real-time polymerase chain reaction (PCR) and cytokine serum concentration by flow cytometry. The average parasitic index of infected dogs was 4.59 × 1010 copies/μl. IL-4 and TNF-α concentrations were higher in infected dogs than in the control group. Antibody levels were positively correlated with IL-4 expression. There was a significant positive correlation of IL-6 cytokine levels with the evolution of stages I and III. Antibody levels were positively correlated with IL-4 expression. There was a significant positive correlation of IL-6 cytokine levels with the evolution of stages I and III. However, this cytokine can be used as a marker to distinguish between different clinical stages.",reviewType:"peer-reviewed",bibtexUrl:"/chapter/bibtex/70551",risUrl:"/chapter/ris/70551",signatures:"José Nivaldo da Silva, Valéria Régia Franco Sousa, Arleana do Bom Parto Ferreira de Almeida, Adenilda Cristina Honorio-França and Eduardo Luzía França",book:{id:"9025",title:"Parasitology and Microbiology Research",subtitle:null,fullTitle:"Parasitology and Microbiology Research",slug:"parasitology-and-microbiology-research",publishedDate:"June 17th 2020",bookSignature:"Gilberto Antonio Bastidas Pacheco and Asghar Ali Kamboh",coverURL:"https://cdn.intechopen.com/books/images_new/9025.jpg",licenceType:"CC BY 3.0",editedByType:"Edited by",editors:[{id:"238219",title:"Dr.",name:"Gilberto Antonio",middleName:null,surname:"Bastidas Pacheco",slug:"gilberto-antonio-bastidas-pacheco",fullName:"Gilberto Antonio Bastidas Pacheco"}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"}},authors:[{id:"105780",title:"Prof.",name:"Eduardo",middleName:null,surname:"França",fullName:"Eduardo França",slug:"eduardo-franca",email:"elfranca@ufmt.br",position:null,institution:{name:"Universidade Federal de Mato Grosso",institutionURL:null,country:{name:"Brazil"}}},{id:"305312",title:"Prof.",name:"Valeria Regia",middleName:"Franco",surname:"Sousa",fullName:"Valeria Regia Sousa",slug:"valeria-regia-sousa",email:"valeriaregia27@gmail.com",position:null,institution:null},{id:"305313",title:"Prof.",name:"Arleana",middleName:null,surname:"Almeida",fullName:"Arleana Almeida",slug:"arleana-almeida",email:"arleferreira@gmail.com",position:null,institution:null},{id:"315522",title:"Dr.",name:"Jose Nivaldo",middleName:null,surname:"Da Silva",fullName:"Jose Nivaldo Da Silva",slug:"jose-nivaldo-da-silva",email:"pronto.vet@hotmail.com",position:null,institution:null},{id:"315523",title:"Prof.",name:"Adenilda Cristina",middleName:null,surname:"Honorio-França",fullName:"Adenilda Cristina Honorio-França",slug:"adenilda-cristina-honorio-franca",email:"adenildachf@gmail.com",position:null,institution:null}],sections:[{id:"sec_1",title:"1. Introduction",level:"1"},{id:"sec_2",title:"2. Methodological aspects",level:"1"},{id:"sec_2_2",title:"2.1 Animals",level:"2"},{id:"sec_3_2",title:"2.2 Blood and bone marrow sample",level:"2"},{id:"sec_4_2",title:"2.3 Immunochromatographic rapid test: RT DPP® kit",level:"2"},{id:"sec_5_2",title:"2.4 DNA extraction, conventional PCR, and qPCR",level:"2"},{id:"sec_6_2",title:"2.5 Cytokine quantification by flow cytometry",level:"2"},{id:"sec_7_2",title:"2.6 Determination of serum immunoglobulins",level:"2"},{id:"sec_8_2",title:"2.7 Statistical analysis",level:"2"},{id:"sec_10",title:"3. Results",level:"1"},{id:"sec_11",title:"4. Discussion",level:"1"},{id:"sec_12",title:"5. Conclusion",level:"1"},{id:"sec_13",title:"Acknowledgments",level:"1"},{id:"sec_16",title:"Conflict of interest",level:"1"}],chapterReferences:[{id:"B1",body:'\nFerreira GE, dos Santos BN, Dorval ME, Ramos TP, Porrozzi R, Peixoto AA, et al. The genetic structure of Leishmania infantum populations in Brazil and its possible association with the transmission cycle of visceral leishmaniasis. PLoS One. 2012;7:e36242\n'},{id:"B2",body:'\nSaporito L, Giammanco GM, De Grazia S, Colomba C. Visceral leishmaniasis: Host-parasite interactions and clinical presentation in the immunocompetent and in the immunocompromised host. International Journal of Infectious Diseases. 2013;17:e572-e576\n'},{id:"B3",body:'\nMissawa NA, Lima GB. Spatial distribution of Lutzomyia longipalpis (Lutz & Neiva, 1912) and Lutzomyia cruzi (Mangabeira, 1938) in the state of Mato Grosso. Revista da Sociedade Brasileira de Medicina Tropical. 2006;39:337-340\n'},{id:"B4",body:'\nMissawa NA, Veloso MA, Maciel GB, Michalsky EM, Dias ES. Evidence of transmission of visceral leishmaniasis by Lutzomyia cruzi in the municipality of Jaciara, state of Mato Grosso, Brazil. Revista da Sociedade Brasileira de Medicina Tropical. 2011;44:76-78\n'},{id:"B5",body:'\nWorld Health Organization. 2019. Available from: http://www.who.ch [Accessed: November 18, 2019]\n'},{id:"B6",body:'\nFeitosa MM, Day MJ. Current status and management of canine leishmaniasis in Latin America. Research in Veterinary Science. 2019;123:261-272\n'},{id:"B7",body:'\nCarvalho AG, Luz JGG, Rodrigues LD, Dias JVL, Fontes CJF. Factors associated with Leishmania spp. infection in domestic dogs from an emerging area of high endemicity for visceral leishmaniasis in Central-Western Brazil. Research in Veterinary Science. 2019;125:205-211\n'},{id:"B8",body:'\nReis AB, Martins-Filho OA, Teixeira-Carvalho A, Giunchetti RC, Carneiro CM, Mayrink W, et al. Systemic and compartmentalized immune response in canine visceral leishmaniasis. Veterinary Immunology and Immunopathology. 2009;128:87-95\n'},{id:"B9",body:'\nTravi BL, Cordeiro-da-Silva A, Dantas-Torres F, Miró G. Canine visceral leishmaniasis: Diagnosis and management of the reservoir living among us. PLoS Neglected Tropical Diseases. 2018;12:e0006082\n'},{id:"B10",body:'\nReis AB, Teixeira-Carvalho A, Giunchetti RC, Guerra LL, Carvalho MG, Mayrink W, et al. Phenotypic features of circulating leucocytes as immunological markers for clinical status and bone marrow parasite density in dogs naturally infected by Leishmania chagasi. Clinical and Experimental Immunology. 2006;146:303-311\n'},{id:"B11",body:'\nFreitas JC, Nunes-Pinheiro DC, Lopes Neto BE, Santos GJ, Abreu CR, Braga RR, et al. Clinical and laboratory alterations in dogs naturally infected by Leishmania chagasi. Revista da Sociedade Brasileira de Medicina Tropical. 2012;45:24-29\n'},{id:"B12",body:'\nNascimento MSL, Albuquerque TDR, Do-Valle-Matta MA, Caldas IS, Diniz LF, Talvani A, et al. Naturally Leishmania infantum-infected dogs display an overall impairment of chemokine and chemokine receptor expression during visceral leishmaniasis. Veterinary Immunology and Immunopathology. 2013;153:202-208\n'},{id:"B13",body:'\nSilva KL, de Andrade MM, Melo LM, Perosso J, Vasconcelos RO, Munari DP, et al. CD4+FOXP3+ cells produce IL-10 in the spleens of dogs with visceral leishmaniasis. Veterinary Parasitology. 2014;202:313-318\n'},{id:"B14",body:'\nRogers KA, DeKrey GK, Mbow ML, Gillespie RD, Brodskyn CI, Titus RG. Type 1 and type 2 responses to leishmania major. FEMS Microbiology Letters. 2002;209:1-7\n'},{id:"B15",body:'\nCosta ASA, Costa GC, Aquino DMC, Mendonça VRR, Barral A, Barral- Netto M, et al. Cytokines and visceral leishmaniasis: A comparison of plasma cytokine profiles between the clinical forms of visceral leishmaniasis. Memórias do Instituto Oswaldo Cruz. 2012;107:735-739\n'},{id:"B16",body:'\nFerrer L, Solano-Gallego L, Arboix M, Alberola J. Evaluation of the specific immune response in dogs infected by Leishmania infantum. Blackwell Science. 2002:92-99\n'},{id:"B17",body:'\nBaneth G, Koutinas AF, Solano-Gallego L, Bourdeau P, Ferrer L. Canine leishmaniosis—New concepts and insights on an expanding zoonosis: Part one. Trends in Parasitology. 2008;24:324-330\n'},{id:"B18",body:'\nDantas-Torres F, Solano-Gallego L, Baneth G, Ribeiro VM, de Paiva-Cavalcanti M, Otranto D. Canine leishmaniosis in the old and new worlds: Unveiled similarities and differences. Trends in Parasitology. 2012;28:531-538\n'},{id:"B19",body:'\nMS. Secretaria de Vigilância em Saúde. Departamento de Análise de Situação de Saúde.Saúde Brasil 2011: uma análise da situação de saúde e a vigilância da saúde da mulher/Ministério da Saúde, Secretaria de Vigilância em Saúde, Departamento de Análise de Situação de Saúde. – Brasília: 444 p. il. Editora do Ministério da Saúde;2012\n'},{id:"B20",body:'\nMaia C, Campino L. Methods for diagnosis of canine leishmaniasis and immune response to infection. Veterinary Parasitology. 2008;158:274-287\n'},{id:"B21",body:'\nRamos RA, Ramos CA, Santos EM, de Araújo FR, de Carvalho GA, Faustino MA, et al. Quantification of Leishmania infantum DNA in the bone marrow, lymph node and spleen of dogs. Revista Brasileira de Parasitologia Veterinária. 2013;22:346-350\n'},{id:"B22",body:'\nPaiva-Cavalcanti M, de Morais RC, Pessoa-E-Silva R, Trajano-Silva LA, Gonçalves-de-Albuquerque SAC, Tavares DEH, et al. Leishmaniases diagnosis: An update on the use of immunological and molecular tools. Cell and Bioscience. 2015;5:31\n'},{id:"B23",body:'\nSolano-Gallego L, Koutinas A, Miró G, Cardoso L, Pennisi MG, Ferrer L, et al. Directions for the diagnosis, clinical staging, treatment and prevention of canine leishmaniosis. Veterinary Parasitology. 2009;165:1-18\n'},{id:"B24",body:'\nLachaud L, Marchergui-Hammami S, Chabbert E, Dereure J, Dedet JP, Bastien P. Comparison of six PCR methods using peripheral blood for detection of canine visceral leishmaniasis. Journal of Clinical Microbiology. 2002;40:210-215\n'},{id:"B25",body:'\nNoli C, Saridomichelakis MN. An update on the diagnosis and treatment of canine leishmaniosis caused by Leishmania infantum (syn. L. chagasi). Veterinary Journal. 2014;202:425-435\n'},{id:"B26",body:'\nSilva KR, Mendonça VR, Silva KM, Nascimento LF, Mendes-Sousa AF, Pinho FA, et al. Scoring clinical signs can help diagnose canine visceral leishmaniasis in a highly endemic area in Brazil. Memórias do Instituto Oswaldo Cruz. 2017;112:53-63\n'},{id:"B27",body:'\nMeléndez-Lazo A, Ordeix L, Planellas M, Pastor J, Solano-Gallego L. Clinicopathological findings in sick dogs naturally infected with Leishmania infantum: Comparison of five different clinical classification systems. Research in Veterinary Science. 2018;117:18-27\n'},{id:"B28",body:'\nQuaresma PF, Murta SMF, de Castro Ferreira E, da Rocha ACVM, Xavier AAP, Gontijo CMF. Molecular diagnosis of canine visceral leishmaniasis: Identification of Leishmania species by PCR-RFLP and quantification of parasite DNA by real-time PCR. Acta Tropica. 2009;111:289-294\n'},{id:"B29",body:'\nMorais RCS, Costa Oliveira CN, Albuquerque SDCG, Silva LAMT, Pessoa-Silva R, Cruz HLA, et al. Real-time PCR for Leishmania species identification: Evaluation and comparison with classical techniques. Experimental Parasitology. 2016;165:43-50\n'},{id:"B30",body:'\nMohammadiha A, Mohebali M, Haghighi A, Mahdian R, Abadi AR, Zarei Z, et al. Comparison of real-time PCR and conventional PCR with two DNA targets for detection of Leishmania (Leishmania) infantum infection in human and dog blood samples. Experimental Parasitology. 2013;133:89-94\n'},{id:"B31",body:'\nScherer EF, Cantarini DG, Siqueira R, Ribeiro EB, Braga É, Honório-França AC, et al. Cytokine modulation of human blood viscosity from vivax malaria patients. Acta Tropica. 2016;158:139-147\n'},{id:"B32",body:'\nMoreira ML, Dorneles EM, Soares RP, Magalhães CP, Costa-Pereira C, Lage AP, et al. Cross-reactivity of commercially available anti-human monoclonal antibodies with canine cytokines: Establishment of a reliable panel to detect the functional profile of peripheral blood lymphocytes by intracytoplasmic staining. Acta Veterinaria Scandinavica. 2015;57:51\n'},{id:"B33",body:'\nde Lima VM, Peiro JR, de Oliveira Vasconcelos R. IL-6 and TNF-alpha production during active canine visceral leishmaniasis. Veterinary Immunology and Immunopathology. 2007;115:189-193\n'},{id:"B34",body:'\nPinelli E, Killick-Kendrick R, Wagenaar J, Bernadina W, del Real G, Ruitenberg J. Cellular and humoral immune responses in dogs experimentally and naturally infected with Leishmania infantum. Infection and Immunity. 1994;62:229-235\n'},{id:"B35",body:'\nDe Vasconcelos TC, Doyen N, Cavaillon JM, Bruno SF, de Campos MP, de Miranda LH, et al. Cytokine and iNOS profiles in lymph nodes of dogs naturally infected with Leishmania infantum and their association with the parasitic DNA load and clinical and histopathological features. Veterinary Parasitology. 2016;227:8-14\n'},{id:"B36",body:'\nSolcà MS, Andrade BB, Abbehusen MM, Teixeira CR, Khouri R, Valenzuela JG, et al. Circulating biomarkers of immune activation, oxidative stress and inflammation characterize severe canine visceral leishmaniasis. Scientific Reports. 2016;6:32619\n'},{id:"B37",body:'\nChoy E, Rose-John S. Interleukin-6 as a multifunctional regulator: Inflammation, immune response, and fibrosis. Journal of Scleroderma and Related Disorders. 2017;2:S1-S5\n'},{id:"B38",body:'\nLe JM, Vilcek J. Interleukin 6: A multifunctional cytokine regulating immune reactions and the acute phase protein response. Laboratory Investigation. 1989;61:588-602\n'},{id:"B39",body:'\nNascimento MS, Albuquerque TD, Nascimento AF, Caldas IS, Do-Valle-Matta MA, Souto JT, et al. Impairment of interleukin-17A expression in canine visceral leishmaniosis is correlated with reduced interferon-γ and inducible nitric oxide synthase expression. Journal of Comparative Pathology. 2015;153:197-205\n'},{id:"B40",body:'\nMichelin FA, Perri SH, De Lima VM. Evaluation of TNF-α, IL-4, and IL-10 and parasite density in spleen and liver of L. chagasi naturally infected dogs. Annals of Tropical Medicine and Parasitology. 2011;105:373-383\n'},{id:"B41",body:'\nTurchetti AP, da Costa LF, Romão EEL, Fujiwara RT, da Paixão TA, Santos RL. Transcription of innate immunity genes and cytokine secretion by canine macrophages resistant or susceptible to intracellular survival of Leishmania infantum. Veterinary Immunology and Immunopathology. 2015;163:67-76\n'},{id:"B42",body:'\nGiunchetti RC, Mayrink W, Carneiro CM, Corrêa-Oliveira R, Martins-Filho OA, Marques MJ, et al. Histopathological and immuno-histochemical investigations of the hepatic compartment associated with parasitism and serum biochemical changes in canine visceral leishmaniasis. Research in Veterinary Science. 2008;84:269-277\n'},{id:"B43",body:'\nQuinnell RJ, Courtenay O, Shaw MA, Day MJ, Garcez LM, Dye C, et al. Tissue cytokine responses in canine visceral leishmaniasis. The Journal of Infectious Diseases. 2001;183:1421-1424\n'},{id:"B44",body:'\nBrachelente C, Müller N, Doherr MG, Sattler U, Welle M. Cutaneous leishmaniasis in naturally infected dogs is associated with a T helper-2-biased immune response. Veterinary Pathology. 2005;42:166-175\n'},{id:"B45",body:'\nJeronimo SMB, Holst AKB, Jamieson SE, Francis R, Martins DRA, Bezerra FL, et al. Genes at human chromosome 5q31.1 regulate delayed-type hypersensitivity responses associated with Leishmania chagasi infection. Genetics of Immunity. 2007;8:539\n'},{id:"B46",body:'\nRodríguez A, Solano-Gallego L, Ojeda A, Quintana J, Riera C, Gállego M, et al. Dynamics of Leishmania-specific immunoglobulin isotypes in dogs with clinical leishmaniasis before and after treatment. Journal of Veterinary Internal Medicine. 2006;20:495-498\n'},{id:"B47",body:'\nCiaramella P, Oliva G, Luna RD, Gradoni L, Ambrosio R, Cortese L, et al. A retrospective clinical study of canine leishmaniasis in 150 dogs naturally infected by Leishmania infantum. The Veterinary Record. 1997;141:539-543\n'},{id:"B48",body:'\nMedeiros CMO, Melo AGC, Lima AKF, Silva ING, Oliveira LCO, Silva MC. Haematological profile of dogs with visceral leishmaniasis in the city of Fortaleza, Ceará. Ciência Animal. 2008;18:43-50\n'}],footnotes:[],contributors:[{corresp:null,contributorFullName:"José Nivaldo da Silva",address:null,affiliation:'
Faculty of Veterinary Medicine, Federal University of Mato Grosso, Brazil
Institute of Biological and Health Sciences, Federal University of Mato Grosso, Brazil
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Traditional inspection on catenary components has to be performed only at night with human eyes. Not only the inspection speed is very slow but also the inspection results are not reliable, as a result of the poor lighting environment and long-time working tiredness. In this chapter, we present an automatic visual inspection system for checking the status of components on catenary. A dedicated designed camera system is mounted on an inspection car, which covers almost all the components to be checked and gives great details of each component. Considering the great data storm at each catenary post, high-performance servers with GPU acceleration are used, and technologies of multi-thread and parallel computing are exploited. Furthermore, an intelligent analysis framework is proposed, which uses structural analysis to localize each component in the image and perform automatic detection based on different features such as geometry, texture, and logic rules. 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IntechOpen aims to ensure that original material is published while at the same time giving significant freedom to our Authors. To that end we maintain a flexible Copyright Policy guaranteeing that there is no transfer of copyright to the publisher and Authors retain exclusive copyright to their Work.
',metaTitle:"Publication Agreement - Chapters",metaDescription:"IN TECH aims to guarantee that original material is published while at the same time giving significant freedom to our authors. For that matter, we uphold a flexible copyright policy meaning that there is no transfer of copyright to the publisher and authors retain exclusive copyright to their work.\n\nWhen submitting a manuscript the Corresponding Author is required to accept the terms and conditions set forth in our Publication Agreement as follows:",metaKeywords:null,canonicalURL:"/page/publication-agreement-chapters",contentRaw:'[{"type":"htmlEditorComponent","content":"
The Corresponding Author (acting on behalf of all Authors) and INTECHOPEN LIMITED, incorporated and registered in England and Wales with company number 11086078 and a registered office at 5 Princes Gate Court, London, United Kingdom, SW7 2QJ conclude the following Agreement regarding the publication of a Book Chapter:
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The aforementioned licenses shall survive the expiry or termination of this Agreement for any reason.
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All payments shall be due 30 days from the date of the issued invoice. The Corresponding Author or the payer on the Corresponding Author's and Co-Authors' behalf will bear all banking and similar charges incurred.
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The Corresponding Author also warrants and represents that: (i) they have the full power to enter into this Publication Agreement on their own behalf and on behalf of each Co-Author; and (ii) they have the necessary rights and/or title in and to the Chapter to grant IntechOpen, on behalf of themselves and any Co-Author, the rights and licenses expressed to be granted in this Publication Agreement. If the Chapter was prepared jointly by the Corresponding Author and any Co-Author, the Corresponding Author warrants and represents that: (i) each Co-Author agrees to the submission, license and publication of the Chapter on the terms of this Publication Agreement; and (ii) they have the authority to enter into this Publication Agreement on behalf of and bind each Co-Author. The Corresponding Author shall: (i) ensure each Co-Author complies with all relevant provisions of this Publication Agreement, including those relating to confidentiality, performance and standards, as if a party to this Publication Agreement; and (ii) remain primarily liable for all acts and/or omissions of each such Co-Author.
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5. TERMINATION
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5.1 IntechOpen has a right to terminate this Publication Agreement for quality, program, technical or other reasons with immediate effect, including without limitation (i) if the Corresponding Author or any Co-Author commits a material breach of this Publication Agreement; (ii) if the Corresponding Author or any Co-Author (being an individual) is the subject of a bankruptcy petition, application or order; or (iii) if the Corresponding Author or any Co-Author (being a company) commences negotiations with all or any class of its creditors with a view to rescheduling any of its debts, or makes a proposal for or enters into any compromise or arrangement with any of its creditors.
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In case of termination, IntechOpen will notify the Corresponding Author, in writing, of the decision.
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6. INTECHOPEN’S DUTIES AND RIGHTS
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6.1 Unless prevented from doing so by events outside its reasonable control, IntechOpen, in its discretion, agrees to publish the Chapter attributing it to the Corresponding Author and any Co-Author.
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6.2 IntechOpen has the right to use the Corresponding Author’s and any Co-Author’s names and likeness in connection with scientific dissemination, retrieval, archiving, web hosting and promotion and marketing of the Chapter and has the right to contact the Corresponding Author and any Co-Author until the Chapter is publicly available on any platform owned and/or operated by IntechOpen.
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6.3 IntechOpen is granted the authority to enforce the rights from this Publication Agreement, on behalf of the Corresponding Author and any Co-Author, against third parties (for example in cases of plagiarism or copyright infringements). In respect of any such infringement or suspected infringement of the copyright in the Chapter, IntechOpen shall have absolute discretion in addressing any such infringement which is likely to affect IntechOpen's rights under this Publication Agreement, including issuing and conducting proceedings against the suspected infringer.
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7.3 Entire Agreement: This Publication Agreement constitutes the entire agreement between the parties in relation to its subject matter. It replaces and extinguishes all prior agreements, draft agreements, arrangements, collateral warranties, collateral contracts, statements, assurances, representations and undertakings of any nature made by or on behalf of the parties, whether oral or written, in relation to that subject matter. Each party acknowledges that in entering into this Publication Agreement it has not relied upon any oral or written statements, collateral or other warranties, assurances, representations or undertakings which were made by or on behalf of the other party in relation to the subject matter of this Publication Agreement at any time before its signature (together "Pre-Contractual Statements"), other than those which are set out in this Publication Agreement. Each party hereby waives all rights and remedies which might otherwise be available to it in relation to such Pre-Contractual Statements. Nothing in this clause shall exclude or restrict the liability of either party arising out of its pre-contract fraudulent misrepresentation or fraudulent concealment.
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7.4 Waiver: No failure or delay by a party to exercise any right or remedy provided under this Publication Agreement or by law shall constitute a waiver of that or any other right or remedy, nor shall it preclude or restrict the further exercise of that or any other right or remedy. No single or partial exercise of such right or remedy shall preclude or restrict the further exercise of that or any other right or remedy.
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7.8 Governing law: This Publication Agreement and any dispute or claim (including non-contractual disputes or claims) arising out of or in connection with it or its subject matter or formation shall be governed by and construed in accordance with the law of England and Wales. The parties submit to the exclusive jurisdiction of the English courts to settle any dispute or claim arising out of or in connection with this Publication Agreement (including any non-contractual disputes or claims).
The Corresponding Author (acting on behalf of all Authors) and INTECHOPEN LIMITED, incorporated and registered in England and Wales with company number 11086078 and a registered office at 5 Princes Gate Court, London, United Kingdom, SW7 2QJ conclude the following Agreement regarding the publication of a Book Chapter:
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1. DEFINITIONS
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Corresponding Author: The Author of the Chapter who serves as a Signatory to this Agreement. The Corresponding Author acts on behalf of any other Co-Author.
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Co-Author: All other Authors of the Chapter besides the Corresponding Author.
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IntechOpen: IntechOpen Ltd., the Publisher of the Book.
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Book: The publication as a collection of chapters compiled by IntechOpen including the Chapter. Chapter: The original literary work created by Corresponding Author and any Co-Author that is the subject of this Agreement.
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2. CORRESPONDING AUTHOR'S GRANT OF RIGHTS
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2.1 Subject to the following Article, the Corresponding Author grants and shall ensure that each Co-Author grants, to IntechOpen, during the full term of copyright and any extensions or renewals of that term the following:
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An irrevocable, worldwide, royalty-free, perpetual, transferable, sublicensable, non-exclusive right to publish, communicate to the public, reproduce, republish, transmit, sell, distribute and otherwise use and make available the Chapter in whole, partial or adapted from and/or incorporated in or in conjunction with other works, in electronic and print editions of the Publication and in derivative works and on any platform owned and/or operated by IntechOpen, throughout the world, in all languages, and in all media and formats now known or later developed.
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An irrevocable, worldwide, royalty-free, perpetual, transferable, sublicensable, non-exclusive right to create and store electronic archival copies of the Chapter, including the right to deposit the Chapter in open access digital repositories.
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An irrevocable, worldwide, royalty-free, perpetual, transferable, sublicensable, non-exclusive right to license others to reproduce, translate, republish, transmit and distribute the Chapter in whole, partial or adapted from and/or incorporated in or in conjunction with other works under the condition that the Corresponding Author and each Co-Author is attributed (currently this is carried out by publishing the Chapter under a Creative Commons Attribution 3.0 Unported License).
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The aforementioned licenses shall survive the expiry or termination of this Agreement for any reason.
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2.2 The Corresponding Author (on their own behalf and on behalf of any Co-Author) reserves the following rights to the Chapter but agrees not to exercise them in such a way as to adversely affect IntechOpen's ability to utilize the full benefit of this Publication Agreement: (i) reprographic rights worldwide, other than those which subsist in the typographical arrangement of the Chapter as published by IntechOpen; and (ii) public lending rights arising under the Public Lending Right Act 1979, as amended from time to time, and any similar rights arising in any part of the world.
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The Corresponding Author confirms that they (and any Co-Author) are and will remain a member of any applicable licensing and collecting society and any successor to that body responsible for administering royalties for the reprographic reproduction of copyright works.
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Subject to the license granted above, copyright in the Chapter and all versions of it created during IntechOpen's editing process (including the published version) is retained by the Corresponding Author and any Co-Author.
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Subject to the license granted above, the Corresponding Author and any Co-Author retains patent, trademark and other intellectual property rights to the Chapter.
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2.3 All rights granted to IntechOpen in this Article are assignable, sublicensable or otherwise transferrable to third parties without the Corresponding Author's or any Co-Author’s specific approval.
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2.4 The Corresponding Author (on their own behalf and on behalf of each Co-Author) will not assert any rights under the Copyright, Designs and Patents Act 1988 to object to derogatory treatment of the Chapter as a consequence of IntechOpen's changes to the Chapter arising from translation of it, corrections and edits for house style, removal of problematic material and other reasonable edits.
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3. CORRESPONDING AUTHOR'S DUTIES
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3.1 When distributing or re-publishing the Chapter, the Corresponding Author agrees to credit the Book in which the Chapter has been published as the source of first publication, as well as IntechOpen. The Corresponding Author warrants that each Co-Author will also credit the Book in which the Chapter has been published as the source of first publication, as well as IntechOpen, when they are distributing or re-publishing the Chapter.
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3.2 When submitting the Chapter, the Corresponding Author agrees to:
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Comply with all instructions and guidelines provided by IntechOpen;
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Produce the Chapter with all due skill, care and diligence, and in accordance with good scientific practice;
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Submit all the corrections in due time as defined during the publishing process schedule.
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The Corresponding Author will be held responsible for the payment of the Open Access Publishing Fees.
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All payments shall be due 30 days from the date of the issued invoice. The Corresponding Author or the payer on the Corresponding Author's and Co-Authors' behalf will bear all banking and similar charges incurred.
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3.3 The Corresponding Author shall obtain in writing all consents necessary for the reproduction of any material in which a third-party right exists, including quotations, photographs and illustrations, in all editions of the Chapter worldwide for the full term of the above licenses, and shall provide to IntechOpen upon request the original copies of such consents for inspection (at IntechOpen's option) or photocopies of such consents.
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The Corresponding Author shall obtain written informed consent for publication from people who might recognize themselves or be identified by others (e.g. from case reports or photographs).
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3.4 The Corresponding Author and any Co-Author shall respect confidentiality rights during and after the termination of this Agreement. The information contained in all correspondence and documents as part of the publishing activity between IntechOpen and the Corresponding Author and any Co-Author are confidential and are intended only for the recipient. The contents may not be disclosed publicly and are not intended for unauthorized use or distribution. Any use, disclosure, copying, or distribution is prohibited and may be unlawful.
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4. CORRESPONDING AUTHOR'S WARRANTY
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4.1 The Corresponding Author represents and warrants that the Chapter does not and will not breach any applicable law or the rights of any third party and, specifically, that the Chapter contains no matter that is defamatory or that infringes any literary or proprietary rights, intellectual property rights, or any rights of privacy. The Corresponding Author warrants and represents that: (i) the Chapter is the original work of themselves and any Co-Author and is not copied wholly or substantially from any other work or material or any other source; (ii) the Chapter has not been formally published in any other peer-reviewed journal or in a book or edited collection, and is not under consideration for any such publication; (iii) they themselves and any Co-Author are qualifying persons under section 154 of the Copyright, Designs and Patents Act 1988; (iv) they themselves and any Co-Author have not assigned and will not during the term of this Publication Agreement purport to assign any of the rights granted to IntechOpen under this Publication Agreement; and (v) the rights granted by this Publication Agreement are free from any security interest, option, mortgage, charge or lien.
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The Corresponding Author also warrants and represents that: (i) they have the full power to enter into this Publication Agreement on their own behalf and on behalf of each Co-Author; and (ii) they have the necessary rights and/or title in and to the Chapter to grant IntechOpen, on behalf of themselves and any Co-Author, the rights and licenses expressed to be granted in this Publication Agreement. If the Chapter was prepared jointly by the Corresponding Author and any Co-Author, the Corresponding Author warrants and represents that: (i) each Co-Author agrees to the submission, license and publication of the Chapter on the terms of this Publication Agreement; and (ii) they have the authority to enter into this Publication Agreement on behalf of and bind each Co-Author. The Corresponding Author shall: (i) ensure each Co-Author complies with all relevant provisions of this Publication Agreement, including those relating to confidentiality, performance and standards, as if a party to this Publication Agreement; and (ii) remain primarily liable for all acts and/or omissions of each such Co-Author.
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The Corresponding Author agrees to indemnify and hold IntechOpen harmless against all liabilities, costs, expenses, damages and losses and all reasonable legal costs and expenses suffered or incurred by IntechOpen arising out of or in connection with any breach of the aforementioned representations and warranties. This indemnity shall not cover IntechOpen to the extent that a claim under it results from IntechOpen's negligence or willful misconduct.
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4.2 Nothing in this Publication Agreement shall have the effect of excluding or limiting any liability for death or personal injury caused by negligence or any other liability that cannot be excluded or limited by applicable law.
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5. TERMINATION
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5.1 IntechOpen has a right to terminate this Publication Agreement for quality, program, technical or other reasons with immediate effect, including without limitation (i) if the Corresponding Author or any Co-Author commits a material breach of this Publication Agreement; (ii) if the Corresponding Author or any Co-Author (being an individual) is the subject of a bankruptcy petition, application or order; or (iii) if the Corresponding Author or any Co-Author (being a company) commences negotiations with all or any class of its creditors with a view to rescheduling any of its debts, or makes a proposal for or enters into any compromise or arrangement with any of its creditors.
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In case of termination, IntechOpen will notify the Corresponding Author, in writing, of the decision.
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6. INTECHOPEN’S DUTIES AND RIGHTS
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6.1 Unless prevented from doing so by events outside its reasonable control, IntechOpen, in its discretion, agrees to publish the Chapter attributing it to the Corresponding Author and any Co-Author.
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6.2 IntechOpen has the right to use the Corresponding Author’s and any Co-Author’s names and likeness in connection with scientific dissemination, retrieval, archiving, web hosting and promotion and marketing of the Chapter and has the right to contact the Corresponding Author and any Co-Author until the Chapter is publicly available on any platform owned and/or operated by IntechOpen.
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6.3 IntechOpen is granted the authority to enforce the rights from this Publication Agreement, on behalf of the Corresponding Author and any Co-Author, against third parties (for example in cases of plagiarism or copyright infringements). In respect of any such infringement or suspected infringement of the copyright in the Chapter, IntechOpen shall have absolute discretion in addressing any such infringement which is likely to affect IntechOpen's rights under this Publication Agreement, including issuing and conducting proceedings against the suspected infringer.
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7. MISCELLANEOUS
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7.1 Further Assurance: The Corresponding Author shall and will ensure that any relevant third party (including any Co-Author) shall, execute and deliver whatever further documents or deeds and perform such acts as IntechOpen reasonably requires from time to time for the purpose of giving IntechOpen the full benefit of the provisions of this Publication Agreement.
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7.2 Third Party Rights: A person who is not a party to this Publication Agreement may not enforce any of its provisions under the Contracts (Rights of Third Parties) Act 1999.
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7.3 Entire Agreement: This Publication Agreement constitutes the entire agreement between the parties in relation to its subject matter. It replaces and extinguishes all prior agreements, draft agreements, arrangements, collateral warranties, collateral contracts, statements, assurances, representations and undertakings of any nature made by or on behalf of the parties, whether oral or written, in relation to that subject matter. Each party acknowledges that in entering into this Publication Agreement it has not relied upon any oral or written statements, collateral or other warranties, assurances, representations or undertakings which were made by or on behalf of the other party in relation to the subject matter of this Publication Agreement at any time before its signature (together "Pre-Contractual Statements"), other than those which are set out in this Publication Agreement. Each party hereby waives all rights and remedies which might otherwise be available to it in relation to such Pre-Contractual Statements. Nothing in this clause shall exclude or restrict the liability of either party arising out of its pre-contract fraudulent misrepresentation or fraudulent concealment.
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7.4 Waiver: No failure or delay by a party to exercise any right or remedy provided under this Publication Agreement or by law shall constitute a waiver of that or any other right or remedy, nor shall it preclude or restrict the further exercise of that or any other right or remedy. No single or partial exercise of such right or remedy shall preclude or restrict the further exercise of that or any other right or remedy.
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7.5 Variation: No variation of this Publication Agreement shall be effective unless it is in writing and signed by the parties (or their duly authorized representatives).
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7.6 Severance: If any provision or part-provision of this Publication Agreement is or becomes invalid, illegal or unenforceable, it shall be deemed modified to the minimum extent necessary to make it valid, legal and enforceable. If such modification is not possible, the relevant provision or part-provision shall be deemed deleted.
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Any modification to or deletion of a provision or part-provision under this clause shall not affect the validity and enforceability of the rest of this Publication Agreement.
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7.7 No partnership: Nothing in this Publication Agreement is intended to, or shall be deemed to, establish or create any partnership or joint venture or the relationship of principal and agent or employer and employee between IntechOpen and the Corresponding Author or any Co-Author, nor authorize any party to make or enter into any commitments for or on behalf of any other party.
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7.8 Governing law: This Publication Agreement and any dispute or claim (including non-contractual disputes or claims) arising out of or in connection with it or its subject matter or formation shall be governed by and construed in accordance with the law of England and Wales. The parties submit to the exclusive jurisdiction of the English courts to settle any dispute or claim arising out of or in connection with this Publication Agreement (including any non-contractual disputes or claims).
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Last updated: 2020-11-27
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