Lectin families in nature.
\\n\\n
More than half of the publishers listed alongside IntechOpen (18 out of 30) are Social Science and Humanities publishers. IntechOpen is an exception to this as a leader in not only Open Access content but Open Access content across all scientific disciplines, including Physical Sciences, Engineering and Technology, Health Sciences, Life Science, and Social Sciences and Humanities.
\\n\\nOur breakdown of titles published demonstrates this with 47% PET, 31% HS, 18% LS, and 4% SSH books published.
\\n\\n“Even though ItechOpen has shown the potential of sci-tech books using an OA approach,” other publishers “have shown little interest in OA books.”
\\n\\nAdditionally, each book published by IntechOpen contains original content and research findings.
\\n\\nWe are honored to be among such prestigious publishers and we hope to continue to spearhead that growth in our quest to promote Open Access as a true pioneer in OA book publishing.
\\n\\n\\n\\n
\\n"}]',published:!0,mainMedia:null},components:[{type:"htmlEditorComponent",content:'
Simba Information has released its Open Access Book Publishing 2020 - 2024 report and has again identified IntechOpen as the world’s largest Open Access book publisher by title count.
\n\nSimba Information is a leading provider for market intelligence and forecasts in the media and publishing industry. The report, published every year, provides an overview and financial outlook for the global professional e-book publishing market.
\n\nIntechOpen, De Gruyter, and Frontiers are the largest OA book publishers by title count, with IntechOpen coming in at first place with 5,101 OA books published, a good 1,782 titles ahead of the nearest competitor.
\n\nSince the first Open Access Book Publishing report published in 2016, IntechOpen has held the top stop each year.
\n\n\n\nMore than half of the publishers listed alongside IntechOpen (18 out of 30) are Social Science and Humanities publishers. IntechOpen is an exception to this as a leader in not only Open Access content but Open Access content across all scientific disciplines, including Physical Sciences, Engineering and Technology, Health Sciences, Life Science, and Social Sciences and Humanities.
\n\nOur breakdown of titles published demonstrates this with 47% PET, 31% HS, 18% LS, and 4% SSH books published.
\n\n“Even though ItechOpen has shown the potential of sci-tech books using an OA approach,” other publishers “have shown little interest in OA books.”
\n\nAdditionally, each book published by IntechOpen contains original content and research findings.
\n\nWe are honored to be among such prestigious publishers and we hope to continue to spearhead that growth in our quest to promote Open Access as a true pioneer in OA book publishing.
\n\n\n\n
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by"}},authors:[{id:"119775",title:"Prof.",name:"Osman",middleName:null,surname:"Babaarslan",fullName:"Osman Babaarslan",slug:"osman-babaarslan",email:"teksob@cu.edu.tr",position:null,institution:{name:"Cukurova University",institutionURL:null,country:{name:"Turkey"}}},{id:"178353",title:"Dr.",name:"Halil",middleName:"İbrahim",surname:"Çelik",fullName:"Halil Çelik",slug:"halil-celik",email:"hcelik@gantep.edu.tr",position:null,institution:{name:"Gaziantep University",institutionURL:null,country:{name:"Turkey"}}},{id:"216179",title:"Dr.",name:"Esin",middleName:null,surname:"Sarıoğlu",fullName:"Esin Sarıoğlu",slug:"esin-sarioglu",email:"sarioglu@gantep.edu.tr",position:null,institution:{name:"Gaziantep University",institutionURL:null,country:{name:"Turkey"}}},{id:"245674",title:"Mrs.",name:"Münevver",middleName:null,surname:"Ertek Avci",fullName:"Münevver Ertek Avci",slug:"munevver-ertek-avci",email:"Munevver.ErtekAvci@calikdenim.com",position:null,institution:null}]},book:{id:"7242",title:"Engineered Fabrics",subtitle:null,fullTitle:"Engineered Fabrics",slug:"engineered-fabrics",publishedDate:"February 13th 2019",bookSignature:"Mukesh Kumar Singh",coverURL:"https://cdn.intechopen.com/books/images_new/7242.jpg",licenceType:"CC BY 3.0",editedByType:"Edited by",editors:[{id:"36895",title:"Dr.",name:"Mukesh Kumar",middleName:null,surname:"Singh",slug:"mukesh-kumar-singh",fullName:"Mukesh Kumar Singh"}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"}}},ofsBook:{item:{type:"book",id:"8807",leadTitle:null,title:"Organic Synthesis",subtitle:null,reviewType:"peer-reviewed",abstract:"
\r\n\tOrganic synthesis has always been one of the central topics of research for the scientific community in the academic laboratories and industrial world. Many striking journal articles and remarkable reviews and books have been published in the past year describing the practicability and applications of the subject demonstrating the importance of organic synthesis. In the present book, we will be putting together the topics in organic synthesis which may include but not limited to, (1) the basic terms and concepts, (2) various organic reactions including reduction, oxidation, addition, elimination, rearrangements, and cycloadditions, (3) Total Synthesis of Natural products, (4) transition metal catalysts, organocatalysts, enzymes and biotransformations, (5) applications in medicinal chemistry and drug design and development, (6) purification methods and characterization techniques, etc. To set a limit and to increase the scope of the book, author(s) are encouraged to send the chapters that include selected examples with practical applications and good yielding reactions reported within the past decade. Older topics with significant findings or their essence to prepare the foundation may be included in the chapter are welcomed as well.
",isbn:null,printIsbn:"979-953-307-X-X",pdfIsbn:null,doi:null,price:0,priceEur:null,priceUsd:null,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"f3bbbd989d0896f142d317ccb8abcc35",bookSignature:"Dr. Prashant S Deore",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/8807.jpg",keywords:"Natural Product Synthesis, Organic Reaction Mechanism, Stereoselective synthesis, Chirality, C-H Functionalization, Cross-Coupling Reactions, Heterogeneous Catalysis, Homogeneous Catalysis, Green Synthesis, Green Solvents and Reagents, Bioorganic synthesis, Click Chemistry",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:0,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"December 10th 2018",dateEndSecondStepPublish:"January 14th 2019",dateEndThirdStepPublish:"March 15th 2019",dateEndFourthStepPublish:"May 20th 2019",dateEndFifthStepPublish:"July 19th 2019",remainingDaysToSecondStep:"2 years",secondStepPassed:!0,currentStepOfPublishingProcess:5,editedByType:null,kuFlag:!1,biosketch:null,coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"251769",title:"Dr.",name:"Prashant",middleName:"S",surname:"Deore",slug:"prashant-deore",fullName:"Prashant Deore",profilePictureURL:"https://mts.intechopen.com/storage/users/251769/images/system/251769.png",biography:"Dr. Prashant S. Deore was born in India. He received a Master’s degree in organic chemistry from Pune University in 2007. In the same year, he qualified with the SET and CSIR-NET (JRF) and joined in the group of Prof. Narshinha P. Argade for the doctoral studies in National Chemical Laboratory, India. In 2014, he awarded with a Ph. D. in Chemistry and was a recipient of the 2nd prize in “2014 Eli Lilly and Company Asia Outstanding Thesis Awards”. In July 2014 he moved to Canada and joined as a postdoctoral researcher in the group of Prof. Richard Manderville at the University of Guelph, Canada. Presently, Dr. Deore is working on the collaborative project between the University of Guelph and Aterica health Inc., and providing consulting to the company. His research interest includes organic synthesis, fluorescent probes development, nucleic acid synthesis and modifications, and aptasensor development for proteins and food toxins.",institutionString:"University of Guelph",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"0",totalChapterViews:"0",totalEditedBooks:"0",institution:null}],coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"8",title:"Chemistry",slug:"chemistry"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"270935",firstName:"Rozmari",lastName:"Marijan",middleName:null,title:"Ms.",imageUrl:"https://mts.intechopen.com/storage/users/270935/images/7974_n.png",email:"rozmari@intechopen.com",biography:"As an Author Service Manager my responsibilities include monitoring and facilitating all publishing activities for authors and editors. From chapter submission and review, to approval and revision, copyediting and design, until final publication, I work closely with authors and editors to ensure a simple and easy publishing process. I maintain constant and effective communication with authors, editors and reviewers, which allows for a level of personal support that enables contributors to fully commit and concentrate on the chapters they are writing, editing, or reviewing. I assist authors in the preparation of their full chapter submissions and track important deadlines and ensure they are met. I help to coordinate internal processes such as linguistic review, and monitor the technical aspects of the process. As an ASM I am also involved in the acquisition of editors. Whether that be identifying an exceptional author and proposing an editorship collaboration, or contacting researchers who would like the opportunity to work with IntechOpen, I establish and help manage author and editor acquisition and contact."}},relatedBooks:[{type:"book",id:"1591",title:"Infrared Spectroscopy",subtitle:"Materials Science, Engineering and Technology",isOpenForSubmission:!1,hash:"99b4b7b71a8caeb693ed762b40b017f4",slug:"infrared-spectroscopy-materials-science-engineering-and-technology",bookSignature:"Theophile Theophanides",coverURL:"https://cdn.intechopen.com/books/images_new/1591.jpg",editedByType:"Edited by",editors:[{id:"37194",title:"Dr.",name:"Theophanides",surname:"Theophile",slug:"theophanides-theophile",fullName:"Theophanides Theophile"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3092",title:"Anopheles mosquitoes",subtitle:"New insights into malaria vectors",isOpenForSubmission:!1,hash:"c9e622485316d5e296288bf24d2b0d64",slug:"anopheles-mosquitoes-new-insights-into-malaria-vectors",bookSignature:"Sylvie Manguin",coverURL:"https://cdn.intechopen.com/books/images_new/3092.jpg",editedByType:"Edited by",editors:[{id:"50017",title:"Prof.",name:"Sylvie",surname:"Manguin",slug:"sylvie-manguin",fullName:"Sylvie Manguin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3161",title:"Frontiers in Guided Wave Optics and Optoelectronics",subtitle:null,isOpenForSubmission:!1,hash:"deb44e9c99f82bbce1083abea743146c",slug:"frontiers-in-guided-wave-optics-and-optoelectronics",bookSignature:"Bishnu Pal",coverURL:"https://cdn.intechopen.com/books/images_new/3161.jpg",editedByType:"Edited by",editors:[{id:"4782",title:"Prof.",name:"Bishnu",surname:"Pal",slug:"bishnu-pal",fullName:"Bishnu Pal"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"72",title:"Ionic Liquids",subtitle:"Theory, Properties, New Approaches",isOpenForSubmission:!1,hash:"d94ffa3cfa10505e3b1d676d46fcd3f5",slug:"ionic-liquids-theory-properties-new-approaches",bookSignature:"Alexander Kokorin",coverURL:"https://cdn.intechopen.com/books/images_new/72.jpg",editedByType:"Edited by",editors:[{id:"19816",title:"Prof.",name:"Alexander",surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"1373",title:"Ionic Liquids",subtitle:"Applications and Perspectives",isOpenForSubmission:!1,hash:"5e9ae5ae9167cde4b344e499a792c41c",slug:"ionic-liquids-applications-and-perspectives",bookSignature:"Alexander Kokorin",coverURL:"https://cdn.intechopen.com/books/images_new/1373.jpg",editedByType:"Edited by",editors:[{id:"19816",title:"Prof.",name:"Alexander",surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"57",title:"Physics and Applications of Graphene",subtitle:"Experiments",isOpenForSubmission:!1,hash:"0e6622a71cf4f02f45bfdd5691e1189a",slug:"physics-and-applications-of-graphene-experiments",bookSignature:"Sergey Mikhailov",coverURL:"https://cdn.intechopen.com/books/images_new/57.jpg",editedByType:"Edited by",editors:[{id:"16042",title:"Dr.",name:"Sergey",surname:"Mikhailov",slug:"sergey-mikhailov",fullName:"Sergey Mikhailov"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"371",title:"Abiotic Stress in Plants",subtitle:"Mechanisms and Adaptations",isOpenForSubmission:!1,hash:"588466f487e307619849d72389178a74",slug:"abiotic-stress-in-plants-mechanisms-and-adaptations",bookSignature:"Arun Shanker and B. Venkateswarlu",coverURL:"https://cdn.intechopen.com/books/images_new/371.jpg",editedByType:"Edited by",editors:[{id:"58592",title:"Dr.",name:"Arun",surname:"Shanker",slug:"arun-shanker",fullName:"Arun Shanker"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"878",title:"Phytochemicals",subtitle:"A Global Perspective of Their Role in Nutrition and Health",isOpenForSubmission:!1,hash:"ec77671f63975ef2d16192897deb6835",slug:"phytochemicals-a-global-perspective-of-their-role-in-nutrition-and-health",bookSignature:"Venketeshwer Rao",coverURL:"https://cdn.intechopen.com/books/images_new/878.jpg",editedByType:"Edited by",editors:[{id:"82663",title:"Dr.",name:"Venketeshwer",surname:"Rao",slug:"venketeshwer-rao",fullName:"Venketeshwer Rao"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"4816",title:"Face Recognition",subtitle:null,isOpenForSubmission:!1,hash:"146063b5359146b7718ea86bad47c8eb",slug:"face_recognition",bookSignature:"Kresimir Delac and Mislav Grgic",coverURL:"https://cdn.intechopen.com/books/images_new/4816.jpg",editedByType:"Edited by",editors:[{id:"528",title:"Dr.",name:"Kresimir",surname:"Delac",slug:"kresimir-delac",fullName:"Kresimir Delac"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3621",title:"Silver Nanoparticles",subtitle:null,isOpenForSubmission:!1,hash:null,slug:"silver-nanoparticles",bookSignature:"David Pozo Perez",coverURL:"https://cdn.intechopen.com/books/images_new/3621.jpg",editedByType:"Edited by",editors:[{id:"6667",title:"Dr.",name:"David",surname:"Pozo",slug:"david-pozo",fullName:"David Pozo"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"60115",title:"Plant Lectins with Insecticidal and Insectistatic Activities",doi:"10.5772/intechopen.74962",slug:"plant-lectins-with-insecticidal-and-insectistatic-activities",body:'\nLectins are glycoproteins of nonimmune origin that recognize and bind carbohydrates. These proteins are found in a wide variety of species (viruses, bacteria, fungi, seaweed, animals, and plants). This review is mainly based on information of plant lectins that have been found as important new agents in biological control. Plant lectins have been widely studied, and in this group, the legume lectins have been related to insecticidal and insectistatic activities. In addition, Phaseolus vulgaris (PHA), Glechoma hederacea (Gleheda), Canavalia ensiformis (ConA), Griffonia simplicifolia (GSII), and Pisum sativum (PSA) lectins and other legume and Lamiaceae lectins have been studied by the Protein Research Group (PRG) in Colombia. It was evidenced that plant legume lectin domains have structural features characterized by a high percentage of β-sheet structures associated with dimeric or tetrameric assembly, presenting several specific sugar recognition sites, including mannose. In addition to these features, these lectins can interact with the digestive system of insect pests and produce a decrease in intestinal absorption capacity.
\nLectins are proteins or glycoproteins of the nonimmune origin with specific binding affinity for the carbohydrate moiety of glycoconjugates [1]. Lectins comprise a structurally diverse class of proteins characterized by their ability to selectively bind carbohydrate moieties of the glycoproteins of the cell surface. Lectins may be obtained from plant, microbial, or animal sources and may be soluble or membrane bound [2]. In nature, lectins play a role in biological recognition phenomena involving cells and proteins and thereby protect plants against external pathogens such as fungi and other organisms. The ability to bind and agglutinate red blood cells is well known and used for blood typing; hence, the lectins are commonly called hemagglutinins [3].
\nThe term lectin is derived from the Latin word legere meaning “to choose” or “select” and has been generalized to encompass all nonimmune carbohydrate-specific agglutinins regardless of blood type specificity or source. Lectins were initially found and described in plants, but in subsequent years, multiple lectins were isolated from microorganisms and also from animals [4]. Interestingly, plant and animal lectins show no primary structural homology, but they demonstrate similar preferential binding to carbohydrates [5]. This suggests that animal and plant lectin genes may have coevolved, thus highlighting the importance of lectin-carbohydrate interactions in living systems [6].
\nBased on the amino acid sequences of available lectins, it is deduced that the carbohydrate-binding property of most lectins resides in a polypeptide sequence, which is termed as “carbohydrate-recognition domain” [7]. The binding with simple or complex carbohydrate conjugates is reversible and non-covalent. The specificity of lectins toward carbohydrates can be defined on the basis of “hapten inhibition test,” in which various sugars or saccharides are tested for their capacity to inhibit the property of hemagglutination of erythrocytes [8].
\nLectins have been classified according to different features such as source (animal, vegetal, fungal, viral), carbohydrate affinity (mannose, glucose, galactose, fucose, sialic acid), number, and specificity of carbohydrate recognition domains (merolectins, hololectins, chimerolectins, and superlectins) [9]. However, current classification is based on 3D structure and is related to 48 families (Table 1) [10].
\nDistribution | \n||||||||
---|---|---|---|---|---|---|---|---|
No. | \nFamily | \nFold | \nAssembly | \nAnimal | \nPlant | \nFungi | \nBacteria | \nVirus | \n
1 | \nL-type | \nJelly roll | \nDimer | \nx | \nx | \nx | \n\n | \n |
L-type-like | \nJelly roll | \nMonomer | \nx | \nx | \nx | \n\n | \n | |
2 | \nGalectin | \nJelly roll | \nMonomer, dimer | \nx | \n\n | x | \n\n | x | \n
3 | \nPentaxim | \nJelly roll | \nPentamer | \nx | \n\n | \n | \n | \n |
4 | \nI-type | \nIg-like β-sandwich | \nLinked to different domains | \nx | \n\n | \n | \n | \n |
5 | \nC-type | \nα/β-fold | \nLinked to different domains | \nx | \n\n | \n | \n | \n |
6 | \nHyaladherin | \nα/β-fold | \nLinked to different domains | \nx | \n\n | \n | \n | \n |
7 | \nChitinase-like | \n(β/α)8-Barrel | \nMonomer | \nx | \nx | \nx | \nx | \nx | \n
8 | \nM-type | \n(α/α)7-Barrel | \nMonomer | \nx | \nx | \nx | \nx | \n\n |
9 | \nR-type | \nβ-Trefoil | \nLinked to enzyme | \nx | \nx | \nx | \nx | \n\n |
R-type-like | \nβ-Trefoil | \nLinked to different domains | \n\n | \n | x | \nx | \n\n | |
10 | \nACA-like | \nβ-Trefoil | \nDimer | \n\n | x | \n\n | \n | \n |
11 | \nBotulinum neurotoxin-like | \nβ-Trefoil | \nLinked to different domains | \n\n | \n | \n | x | \n\n |
12 | \nF-box | \nJelly roll | \nLinked to different domains | \nx | \n\n | \n | \n | \n |
13 | \nF-type | \nJelly roll | \nLinked to different domains | \nx | \nx | \nx | \nx | \n\n |
14 | \nPA-LL-like | \nJelly roll | \nDimer | \n\n | \n | \n | x | \n\n |
15 | \nP-type | \nα/β-fold | \nDimer | \nx | \n\n | \n | \n | \n |
16 | \nFicolins | \nFibrinogen-like | \nTrimer | \nx | \n\n | \n | \n | \n |
17 | \nMalectin | \nJelly roll | \nMonomer | \nx | \n\n | \n | \n | \n |
18 | \nCalnexin | \nJelly roll | \nMonomer | \nx | \n\n | \n | \n | \n |
19 | \nTachylectin-2-like | \n5-Bladed β-propeller | \nMonomer | \nx | \n\n | \n | \n | \n |
20 | \nTachycitin-like | \nβ-sheet-cysteine fold | \nMonomer | \nx | \n\n | \n | \n | \n |
21 | \nHevein | \nCystine-knot motif | \nDimer | \nx | \nx | \n\n | \n | \n |
22 | \nJacalin-related | \nβ-Prism I | \nTetramer | \nx | \nx | \n\n | \n | \n |
23 | \nSUEL-related | \nα/β-fold | \nLinked to different domains | \nx | \n\n | \n | \n | \n |
24 | \nH-type | \nSix-stranded antiparallel β-sandwich | \nHexamer | \nx | \nx | \n\n | \n | \n |
25 | \nCystine-knot | \nCystine-knot motif | \n\n | X | \n\n | \n | \n | \n |
26 | \nTgMIC4 | \nα/β-fold | \nTandem repeat | \nx | \n\n | \n | \n | \n |
27 | \nTgMIC1 | \nSialic acid binding protein | \nLinked to different domains | \nx | \n\n | \n | \n | \n |
28 | \nLysM | \nβααβ-Motif | \nTriple repeat | \nx | \nx | \nx | \nx | \n\n |
29 | \nLNP-type | \nα/β-fold | \nMonomer | \nx | \nx | \n\n | x | \n\n |
30 | \nMonocot | \nβ-Prism II | \nMonomer, dimer, tetramer | \n\n | x | \n\n | x | \n\n |
31 | \nABL-like | \nα/β-sandwich | \nDimer, tetramer | \n\n | x | \nx | \n\n | \n |
32 | \nCV-N | \nThree-stranded β-sheet and β-hairpins | \nMonomer | \n\n | x | \nx | \nx | \n\n |
33 | \nPVL-like | \nSeven-bladed β-propeller | \nMonomer | \n\n | \n | x | \n\n | \n |
34 | \nAAL-like | \nSix-bladed β-propeller | \nMonomer | \n\n | \n | x | \nx | \n\n |
35 | \nFlocculins | \nβ-Sandwich | \nMonomer | \n\n | \n | x | \nx | \n\n |
36 | \nPCL-like | \nJelly roll | \nTandem repeat | \n\n | \n | x | \n\n | \n |
37 | \nBC2LCN | \nJellyroll | \nTrimer | \n\n | \n | \n | x | \n\n |
38 | \nStaphylococcal toxin | \nβ-Barrel | \nMonomer | \n\n | \n | \n | x | \n\n |
39 | \nAB5 toxin | \nα/β-fold | \nAB5 | \n\n | \n | \n | x | \n\n |
40 | \nPA-IIL-like | \nβ-Sandwich | \nDimer | \n\n | \n | \n | x | \n\n |
41 | \nMVL | \nα/β-fold | \nDimer | \n\n | \n | \n | x | \n\n |
42 | \nPapG | \nβ-Sandwich | \nLinked to different domains | \n\n | \n | \n | x | \n\n |
43 | \nFimH | \nβ-Sandwich | \nLinked to different domains | \n\n | \n | \n | x | \n\n |
44 | \nF17-G | \nβ-Sandwich | \nLinked to different domains | \n\n | \n | \n | x | \n\n |
45 | \nHemagglutinin | \nJelly roll | \nTrimer | \n\n | \n | \n | \n | x | \n
46 | \nRotavirusVP4 | \nJelly roll | \nVirus capsid | \n\n | \n | \n | \n | x | \n
47 | \nViral proteins | \nβ-Sandwich | \nVirus capsid | \n\n | \n | \n | \n | x | \n
48 | \nKnob domain | \nJelly roll | \nVirus capsid | \n\n | \n | \n | \n | x | \n
Lectin families in nature.
Folding, assembly, and source of each family is shown.
Lectins are mainly present in seeds of plants [4, 8, 9], but they are also identified in vegetative tissues such as bulbs, tubers, rhizomes, roots, bark, stems, fruits, and leaves [11].
\nAs previously mentioned, based on their number domains and their characteristics, plant lectins can be divided into four classes [9]:
Merolectins are lectins that possess a single carbohydrate-binding domain. As a result, the merolectins do not present agglutinating activity.
Hololectins contain two or multivalent carbohydrate-binding sites.
Chimerolectins possess a carbohydrate-binding domain and an additional domain that confers other biological activities.
Superlectins are lectins with two or multivalent carbohydrate domains that are able to recognize structurally unrelated sugars.
However, since 1998, five novel lectin domains have been identified in plants. At present, plant lectins are classified into 12 different families, with distinct carbohydrate-binding domains. The families are Agaricus bisporus agglutinin homologs, amaranthines, class V chitinase homologs, Euonymus europaeus agglutinin family, Galanthus nivalis agglutinin family, proteins with hevein domains, jacalins, proteins with legume lectin domains, LysM domain proteins, the Nicotiana tabacum agglutinin family, and the ricin B family [12].
\nIn general, the three-dimensional structure of lectins is composed of a high content of β-sheets with little contribution from α-helixes. The β-sheets are connected by loops forming antiparallel chains. The stability of dimers and tetramers is conferred by hydrophobic interactions, hydrogen bonds, and salt links [13]. Three regions are formed in carbohydrate-binding site [12, 13, 14]:
The central region is constituted by a conserved core in which residues interact with metallic ions (Mg2+, Mn2+, and Ca2+), required for carbohydrate interactions. This core provides necessary binding energy, but it is not important to the lectin’s carbohydrate specificity.
Some aromatic residues surround the core and occupy variable positions in a horseshoe shape. This region is fully involved in the lectin’s monosaccharide specificity.
Finally, residues with higher variability are located in the outer zone and are involved in interactions with larger oligosaccharide ligands.
The structural features of plant lectins are shown in Figure 1, which is possible to see the high content of β-sheets (Figure 1A) and the structure of a typical carbohydrate recognition domain (Figure 1B).
\nStructural conformation of plant lectins. (A) Pterocarpus angolensis homodimer lectin (PDB code (2PHF)). The β-sheet conformation is the most usual in plant lectins (β-sandwich). (B) The carbohydrate recognition domain (CRD) is highly conserved in plant lectins, according to its specificity.
However, the kind of expressed lectins can have some differences according to the specific tissue or the moment in which the plant is expressing it. A lot of plant lectins are constitutively expressed in high amounts in seeds and vegetative storage tissues where they have been shown to play a role in plant defense [15]. But, plants also express minute amounts of specific lectins as particular responses toward environmental stresses and pathogen attack. In the absence of plant stress, the inducible lectins are not expressed at detectable levels [16]. According that, a central question which has often been asked but up to now not yet been answered definitively is that on the biological function(s) of plant lectins. Several functions have been mentioned, but there is not a final decision about that. However, because of its carbohydrate interactions, lectins have been tested for several biological functions, getting interesting results in some of them. Biological activities are related to immunomodulatory and antitumor [17, 18, 19], antifungal [20, 21, 22, 23], antiparasitic [24, 25, 26], antiproliferative [27, 28, 29, 30], healing process [31, 32, 33], drug delivery [34, 35, 36], as histochemical markers [37, 38, 39], biosensors [40, 41], insecticide [42, 43, 44, 45, 46], etc.
\nThe specific carbohydrate recognition shown by lectins makes them important tools in glycobiology, and, although their physiological role remains unknown, they appear to mediate protein-cell and cell-cell interactions. Lectins are widespread in nature, and most of them have been isolated and characterized from Fabaceae, Gramineae, and Lamiaceae families, among others [47, 48]. Those lectins have been related to insect defense mechanisms, storage proteins, carbohydrate transport, mechanisms of physiological regulation, and mitogenic stimulation processes [49, 50, 51, 52, 53, 54, 55]. The ability of the nitrogen-fixing bacteria rhizobia to form a symbiotic relationship with legumes, in which plant root lectins are involved, is well known. The plant-associated bacteria have important effects on plant health and productivity [56, 57, 58, 59]. Thus biofilm formation on plants is associated with symbiotic and pathogenic responses, and some root lectins promote this process [60]. The lectins could be a good biotechnological alternative in the control of bacterial biofilms for different purposes, for example, clinical applications [61]. In general, plant lectins have been widely used for studying carbohydrates on cell surface, for typing blood groups, isolating glycoconjugates, and detecting changes in normal oligosaccharide synthesis in tumoral disorders and other pathologies [62, 63, 64, 65, 66].
\nLectins from Fabaceae have been extensively studied and have a broad specificity for any carbohydrate moieties regardless of having highly conserved amino acid sequences between different species. These proteins have been for a long time a paradigm in the research of interaction protein-carbohydrate and their relationship structure-function [67, 68]. Available sequences (RCSB PDB, UniProtKB/Swiss-Prot) show 20% similarity and 20% of identical amino acids, and conserved amino acids are in the “binding site” and coordinate metal ions [9]. These proteins generally have two or four identical subunits with a molecular weight around 25 kDa; each one contains a binding site for metal ions. A typical example of dimeric lectins belongs to the Viceae tribe. The tetrameric lectins are present in species of the tribe Diocleae, specific by glucose/mannose. In these tribes, many lectins have been isolated and characterized with some biochemical differences and molecular similarities [47]. Recently, subtribe Diocleinae in the Millettioid legumes have been taxonomically tangled together with the large heterogeneous tribe Phaseoleae; however, a comprehensive molecular phylogenetic analysis based on nuclear and chloroplast markers includes all genera ever referred to Diocleae except for the monospecific Philippine Luzonia, resolving several key generic relationships within the Millettioid legumes and considered classification of Diocleinae subtribe as a tribe with three main clades: Canavalia, Dioclea, and Galactia. Canavalia clade has species gender Canavalia; Dioclea clade includes Dioclea, Cymbosema, Cleobulia and Macropsychanthus; and Galactia clade gender has Galactia, Neorudolphia, Rhodopsis, Bionia, Cratylia, Lackeya, Camptosema, and Collaea [69].
\nThis tribe is widely distributed throughout the neotropics, and several species from the genus Dioclea have been shown to possess a lectin closely related to ConA (lectin type I). The better characterized lectins have been those from D. grandiflora [70, 71], D. lehmanni Diels [72], and D. sericea Kunth [73], among others, all of them belong to the Man/Glc group; their physicochemical properties and structural features are very similar [74].
\nStudies carried out in the PRG have allowed us to find other lectins having distinct structural and functional properties (named lectin type II) from Diocleae lehmanni (DLL), Dioclea sericea (DSL), Dioclea grandiflora (DGL), Canavalia ensiformis (CEL), and Galactia lindenii (GLL) [73, 75, 76, 77]. These lectins are localized in the same cellular compartment as happens in D. lehmanni seeds [78] and have different physicochemical properties; this allow us to question about the physiological role of these proteins. Lectin type II has high affinity toward H type 2 blood group (α-L-Fuc (1–2)-β-D-Gal (1–4)-β-D-GlcNAc-O-R), and the N-terminal region presents a unique sequence hitherto found in some Diocleinae lectins and suggests a functional similarity among this type of lectin which possesses distinctive characteristics differentiating them from “classical” mannose/glucose (Man/Glc) lectins. Taking subunit MW into account, it has been demonstrated that tetrameric forms prevailed in type I lectins, being in fast equilibrium with dimers and monomers whose amount depended upon pH or solution ionic strength [79], while some lectins from type II prevalence dimeric forms (Table 2). Despite their high similarity, these ConA-like (type II) lectins could induce different responses in biological assays; for example, when tested for stimulation of human lymphocyte proliferation in vitro, ConBr had a higher proliferation index than ConA, possibly due to minor changes in binding specificities [80].
\nType | \nSpecies | \nSpecificity | \nMonosaccharide inhibitor | \nErythroagglutination | \nNative (kDa) | \nSubunits (kDa) | \npI | \nReferences | \n
---|---|---|---|---|---|---|---|---|
I | \nD. grandiflora | \nMan/Glc | \nMan, Glc, Fru | \nRabbit | \n100 | \nα:25–α:26; β:13–β:14; γ:8–γ:9 | \n8.6–9 | \n[70, 71] | \n
D. lehmanni | \nMan, Glc, Fru, L-sorbose, Me-α-D-Man, Me-α-D-Glc, trehalose | \nRabbit, A+, O+, B+ | \n\n | α:25.3; β:14; γ:N.D | \n8.0–8.4 | \n[72] | \n||
D. sericea | \nMan, Glc | \nA+, O+, B+ | \n57.7 | \nα:29.9; β:16.5; γ: 13.4 | \n6.6–6.9 | \n[73] | \n||
D. altisima | \nMan, Glc, Fru | \nRabbit | \n100 | \nα:26.3; β:14; γ: 9 | \n8.6–9.0 | \n[131] | \n||
D. violaceae | \nMan, Glc, Fru, maltose | \nRabbit | \n\n | α:29.5; β:15.8; γ: 11.7 | \n\n | [132] | \n||
D. rostrata | \nMan, Glc, Fru | \nRabbit, O+ and B+ | \n\n | α:30.9; β:15.8; γ: 11.7 | \n\n | [67] | \n||
D. lasiophylla | \nMan, Me-α-D-Man, ovalbumin, fetuin | \nRabbit | \n\n | α:25,569; β:12,998; γ: 12,588 | \n\n | [133] | \n||
D. sclerocarpa | \n\n | Glc; Gal | \nRabbit | \n102 | \nα: 25,606; β:12,832; γ:12,752 | \n\n | [134] | \n|
C. ensiformis | \nMan, Me-α-fructofuranoside | \nRabbit | \n96 | \nα:25.5; β:14; γ:12.5 | \n7.1 | \n[67] | \n||
C. mollis | \nGlc, Me-α-D-Man | \nRabbit > A+, O+, B+ | \n\n | α:30; β:16; γ: 14 | \n8.5–8.6 | \n[135] | \n||
C. roseum | \nMan | \nRabbit | \n\n | α:30; β:18; γ: 12 | \n\n | [136] | \n||
G. lindenii | \np-Nitrophenyl-β-D-mannopyranoside, Man | \nA+, O+ | \n100 | \n29; 60 | \n6,5 | \n[77] | \n||
II | \nC. ensiformis | \nH-Type II | \nSucrose, melezitose, lactose | \nA+, O+, B+ | \n57.5 | \n29–30 | \n5.2–5.4 | \n[76] | \n
D. grandiflora | \nSucrose, melezitose, lactose | \nA+, O+, B+ | \n58.9 | \n29–30 | \n5.1–5.4 | \n[76] | \n||
D. lehmanni | \nSucrose, melezitose, lactose | \nA+, O+, B+ > rabbit | \n58.4 | \n29–30 | \n6.5–6.6 | \n[75] | \n||
D. sericea | \nLactose, sucrose, melibiose | \nA+, O+, B+ | \n57.27 | \n26.58–30 | \n5.3–5.7 | \n[73] | \n||
G. lindenii | \nGalNAc, Me-β-Gal, Lactose | \nB+, O+ > A+ | \n104,256 | \n26,064 | \n8.3 | \n[137] | \n||
C. roseum | \nGalNAc and N-acetyl-α-D-lactosamine | \nRabbit | \n65 | \n29 | \n— | \n[138] | \n||
Captosemin | \nN-acetyl-α-D-galactosamine | \nA+, O+, B+ | \n104 | \n26 | \n— | \n[139] | \n
Physicochemical properties of lectins of Diocleae tribe.
Abbreviations: kDa, kilodalton; pI, isoelectric point; H-type II, antigen (α-L-Fuc(1–2)-β-D-Gal(1–4)-β-D-GlcNAc-O-R); Man, mannose; Glc, glucose; Me, methyl; Gal, galactose; Fru, fructose; GalNAc, N-acetyl-α-D-galactosamine.
Lamiaceae lectins have been little studied despite preliminary reports on their ability to recognize the Tn/T antigens [81], normally a cryptic structure in the peptide core of O-glycoproteins and which is widely expressed in several tumors and other disorders such as Tn syndrome and IgA nephropathy [82, 83, 84, 85]. The importance of Thomsen-Friedenreich antigen (TF or T, galactose (Gal) β1,3 GalNAcα-O-serine (Ser)/threonine (Thr)) as well as to its precursor, the Tn antigen, and its sialylated forms (sTn) has been reviewed recently [86, 87, 88, 89, 90, 91]; according to the above, it is important to have alternatives to study these structures such as the lectins and antibodies. However, a word of caution should be given as accumulating evidence, which has shown that mAbs and lectins do not interact with Tn-containing structures in an identical manner. The observed differences have been ascribed to different Tn-density requirements for the interaction to occur [92].
\nDetailed studies have been carried out on a very few Lamiaceae species from the Northern hemisphere’s temperate zone until now [93, 94, 95, 96, 97], and the lectin from Salvia sclarea L. seeds (SSL) was the first to be isolated and partially characterized [94]. By contrast, species from the Neotropical Salvia subgenus Calosphace Benth have been little explored despite their great diversity. A systematic survey has been conducted on species belonging to the Neotropical Calosphace Benth subgenus [98], and certain species naturalized in the New World have also been investigated [99], some having commercial value. Given the abundance of Lamiaceae species in Colombia and the potential biotechnological applications, our group undertook a systematic search for the identification, isolation, and characterization of lectins from selected species with the determination of their biological activities. The lectins from S. palifolia Kunth and Hyptis mutabilis (Rich.) Briq. [100] have been partially characterized, and a detailed work has been done with S. bogotensis Benth and Lepechinia bullata (Kunth) Epling [101, 102].
\nThe importance of these proteins as tools in a variety of biological studies and detection, isolation, structural, and functional properties has been studied, and more recently, T/Tn-specific lectins have been found in the families Amaranthaceae, Fabaceae, Moraceae, and Orchidaceae, among others. The lectins themselves belong to five families of structurally and evolutionarily related proteins (amaranthines, legume lectins, jacalin-related lectins, type 2 ribosome-inactivating proteins, and GNA-related lectins) [103].
\nInterestingly, a lectin type I was found in S. bogotensis Benth. (SBoL-I) and Lepechinia bullata (Kunth) Epling (LBL-I) (such as those found in the tribe Diocleae type I), which recognizes mannose/glucose residues; this fact, together with the molecular properties and highly similar N-terminal regions, led us to propose that lectins type I and type II are two good differentiated groups with structural features proper of legume lectins family, particularly from Diocleae tribe, Salvia, and Lepechinia genders (Table 3) [104]. For these lectins, SDS-PAGE profile was similar to other mannose lectins, a band around 30 kDa with an isoelectric point near to 6.5, and they were able to agglutinate human RBCs from A, B, and O donors. This means that specificity by mannose/glucose moieties or mannose-rich glycan is not a unique feature of any family; conversely, species such as Galanthus nivalis (tribe Galantheae) [105] and Centrolobium microchaete (tribe Dalbergieae) [106], among others, even species from other families such as Moraceae have mannose/glucose lectins [107].
\nMolecular properties | \nGLL-I1 | \nDLL-I2 | \nCRL-I3 | \nCEL-I4 | \nSBoL-I5 | \nLBL-I6 | \n
---|---|---|---|---|---|---|
Mr subunit (kDa)7 | \n29 | \n25, 14 | \nND | \n26.5 | \n30–33 | \n30–34 | \n
Mr protein (kDa)8 | \n100 | \nND | \nND | \n106 | \nND | \nND | \n
SDS-page (kDa) | \n29, 60 | \n25, 14 | \n30, 18, 12 | \n26, 14, 12.5 | \n30, 60 | \n30, 60 | \n
Glycosylation | \nSi | \nND | \nND | \nNo | \nSi | \nSi | \n
Neutral Sugars (%) | \nND | \n1.7–1.9 | \nND | \nND | \nND | \nND | \n
Isoelectric point (PI) | \n6.15 | \n8.0; 8.13 8.3; 8.42 | \nND | \n7.1 | \n6.5 | \n6.5 | \n
Mannose inhibition (mM) | \n150 | \n50 | \n19.5 | \nND | \nND | \nND | \n
Sequence N-terminal | \nND | \nADTIVAVELD SYPNTDIGDPSYPH | \nADTIVAVELD SYPNTDIGDPSYPH | \nADTIVAVELD TYPNTDIGDPSYPH | \nADTIVAVELD | \nADTIVAVELD | \n
Molecular properties of lectins type I from Fabaceae and Lamiaceae families.
Galactia lindenii lectin type -I (GLL-I) [77].
Dioclea lehmanni lectin type I (DLL-I) [72].
Cymbosema roseum lectin type I (CRL-I) [136].
Canavalia ensiformis concanavalin A (CEL-I) [67].
Salvia bogotensis lectin type I (SBoL-I) [104].
Lepechinia bullata lectin type I (LBL-I) [104].
Reduced conditions.
Non-reduced conditions without heat.
ND, non-determined.
There are several evidences for the defensive role of vegetal lectins in protecting plants against insect pests [108, 109, 110], and lectins are currently receiving a significant interest as insecticidal agents against sap-sucking insects including aphids and leaf and plant hoppers, with no effect on human metabolism [111, 112]. Lectins act on insects by binding to glycoproteins present in insect gut epithelium, eventually causing death of insect by inhibiting absorption of nutrients. It was believed that N-linked glycans in insects were exclusively of the high mannose type; therefore, there are great interests, especially in mannose-specific plant lectins, as possible insecticidal or insect-deterring molecules for the new pest management strategies [113, 114]. Nevertheless, the lectins possess different sugar specificities and, considering the variety of glycan structures in the bodies of insects, have many different possible targets. Advances have been made in the knowledge related to glycan diversity and function(s) of protein glycosylation in insects, N-glycosylation, and O-glycosylation, and it postulated that the interference in insect glycosylation appears to be a promising strategy for pest insect control [115]. Therefore, it is difficult to predict the exact mode of action of each lectin and even more difficult to understand the variability in insect toxicity upon exposure to different plant lectins. The use of initial bioassays employing artificial diets has led to the most recent advances, such as plant breeding and the construction of fusion proteins, using lectins for targeting the delivery of toxins and to potentiate expected insecticide effects [116, 117, 118].
\nThe first lectin known for insecticidal activity was Galanthus nivalis agglutinin, which belongs to a superfamily of alpha-D-mannose-specific plant bulb lectins [105, 119]. The mannose-binding lectins have shown strong insecticidal activity against chewing and sap-sucking insects and particularly in controlling aphids [120, 121, 122, 123, 124]. Lectin isolated from bulbs of Phycella australis presented a strong insecticidal activity against the pea aphid and green peach aphid, affecting the survival, feeding behavior, and fecundity of aphids, where Acyrthosiphon pisum proved to be particularly sensitive [125].
\nNo considerable mortality effect of ASA lectins (native or recombinant lectins) was shown on larvae of potato moths (Tecia solanivora); however, recombinant ASAII lectin had an effect on the pupa mortality, which was bigger than the native lectin effect. The effect of lectins on the weight and fertility of adults showed that both lectins had a big effect on fertility when the lectin is used in a low concentration (lower than 0.003 mg/mL), and, in some cases, lectins produced malformations in female adults [126]. Fitches et al. found toxic effects on Acyrthosiphon pisum using both recombinant lectins; however, ASA II was more toxic than ASA I, at the same dose [127].
\nLectins from legume family have shown insectistastic and insecticidal activity [52] (Table 4). The lectins from seeds of Canavalia brasiliensis, Dioclea grandiflora, Dioclea rostrata, Cratylia floribunda, and Phaseolus vulgaris have shown to protect seeds against the beetle Callosobruchus maculatus. In general, the plant lectins are the most potent agents against insect pests of a variety of crops including wheat, rice, tobacco, and potatoes [128]. Canavalia lectins exhibited a range of different toxicities toward Artemia nauplii and bound to a similar area in the digestive tract; differences in spatial arrangement and volume of CRD (carbohydrate recognition domain) may explain the variation of the toxicity showed by each lectin despite the high structural similarity [129]. The sensitivity of different insect species to the insecticidal effects of lectin ingestion is variable, and the binding of a lectin to the gut does not necessarily imply toxicity. Other studies signal that lectins affect various insect hydrolytic enzymes such as glucosidases, phosphatases, and proteases which are involved in digestion, development, growth, and detoxification. To date a great number of studies have shown lectin toxicity in insects belonging to different orders, including Lepidoptera, Coleoptera, and Hemiptera. However, the exact mode of action of lectins in providing resistance against insects remains unclear. The most relevant property of lectin’s anti-insect activity can be related to its interactions with different glycoproteins or glycan structures in insects, which may interfere with a number of physiological processes in these organisms. Lectins possess at least one carbohydrate-binding domain and different sugar specificities, possible targets for lectin binding are numerous, and several mechanisms can be associated (Figure 2).
\nLectin | \nInsect pests | \nActivity | \nReferences | \n
---|---|---|---|
PSA | \nMeligethes aeneus | \nInsecticidal, insectistatic | \n[140] | \n
ConA | \nTarophagous proserpina | \nInsectistatic | \n[141] | \n
Gleheda | \nLeptinotarsa decemlineata | \nInsectistatic | \n[130] | \n
ConA | \nCallosobruchus maculatus | \nInsectistatic | \n[142] | \n
ConA | \nHelicoverpa armigera | \nInsectistastic | \n[143] | \n
GS-II | \nCallosobruchus maculatus | \nInsectistastic | \n[144] | \n
PHA | \nCallosobruchus maculatus | \nInsecticidal | \n[145] | \n
PHA-E | \nEmpoasca fabae | \nInsecticidal | \n[146] | \n
Bmoll | \nAnagasta kuehniella Zabrotes subfasciatus Callosobruchus maculatus Callosobruchus maculatus | \nInsecticidal | \n[147] | \n
DGL | \nC. maculatus | \n\n | [108] | \n
DRL | \n\n | \n | \n |
CFL | \n\n | \n | \n |
Legume lectins domain with insectistatic and insecticidal activity.
Pisum sativum (PSA), Canavalia ensiformis (concanavalin A (ConA)), Glechoma hederacea (Gleheda), GS-II: Griffonia simplicifolia aglutinina, Phaseolus vulgaris (PHA), Bauhinia monandra leaf lectin (bmoll), Dioclea grandiflora (DGL), D. rostrata (DRL), Cratylia floribunda (CFL). Taking from Calvacante et al. [60] and modified.
Possible targets and associated mechanisms of lectin anti-insect activity. Lectins have antinutritional properties by which they interact with several targets in digestive tract and other organs.
Preliminary evidence of Gleheda’s insecticidal activity against Colorado potato beetle larvae (Leptinotarsa decemlineata) has been obtained using a single dose of lectin [130]; it would have been very interesting to carry out dose-response experiments and to assay several insect pests to elucidate whether the lectin was insect specific. Nevertheless, Gleheda’s insecticidal activity stresses the importance of this unusual lectin, begging the question of whether such activity is shared by other Lamiaceae lectins. To date Lamiaceae lectin is unique with known insecticidal activity. The importance of lectins due to their insecticidal properties, isolation of native lectins, and lectin genes could be agronomically important tools for crop plants for developing resistance against insect pests mainly for sap-sucking insect. These proteins are very interesting, and its molecular properties have been well described; however, there is still a long way to study and learn about the mechanisms of these molecules at a physiological and molecular level.
\n“Any sufficiently advanced technology is indistinguishable from magic.”
-Arthur C Clarke
Today, 55% of the world’s population lives in urban areas, and this proportion is expected to reach 68% by 2050 [1]. City governments face the challenge of producing wealth, innovation, health, and sustainability [2], but with an increase in urban populations, these challenges become harder for city governments to manage. For this reason, instead of continuing to use old-fashioned methods, some cities have applied updated, innovative methods to manage such issues in smarter ways [3], much as we do in our daily lives. We have moved from using “dumb” technologies (e.g., a road atlas or telephone) to interacting with “smart” technologies (e.g., personalized journey planning apps on smart phones) that “exist to help us, serve us, to make our lives easier and more interesting” [4].
As internationalization has become a widely discussed topic in recent years [5], the problem of overcrowding of cities is considered a global issue, and smart city applications have spread rapidly worldwide [2]. These applications not only enable city governments to facilitate the routine functions of individuals, buildings, and traffic systems but also enable them to monitor, understand, analyze, and plan cities to improve their efficiency, equity, and quality of life in real time [6]. The concept “smart,” therefore, means the ability to manage the complexity through Big Data, which comes from a variety of sources in a huge volume and in a rapid way. As an example, in their daily lives, individuals check their social media accounts from mobile devices and share or like posts. They also read personalized news and check traffic jams. They then check their e-mail when they arrive at their offices. At lunchtime, they order food using online applications, and they watch personalized videos during free time. In other words, individuals produce a great deal of personal data and consume many more services based on that data. Thus, they also desire cities that support this lifestyle [7].
For instance, in Milton Keynes, a large town in the middle of England, the rapid expansion of the Internet together with young and technically inclined population gave rise to the concept of “smart cities.” This included the application of technology, especially Big Data principles, to improve residents’ quality of life. Such applications ranged from waste management to public transportation [8]. Now, many more cities, such as London, Stockholm, Amsterdam, Vienna, Luxembourg, Turku, Eindhoven, and Montpellier, have adopted a “smart” approach. The smart city theme also provides a city more stable and higher brand equity than green and creative themes [9]. In a project conducted at the Vienna University of Technology, six indicators of smart cities were identified:
“Smart economy,” including competitive components, such as innovation, entrepreneurship, and productivity
“Smart people,” which is the result of ethnic or social diversity and related to online education to raise social capital and qualification
“Smart governance,” such as e-government, which can include all parties in transparent decision-making processes
“Smart mobility,” which includes transportation planned using information and communications technologies (ICT)
“Smart environment,” which encourages cities to use energy efficiently by employing innovative technologies, such as solar energy and other renewable sources
“Smart living,” which refers to systems that improve quality of life, such as services and public safety tools [10]
These components are associated with different aspects of urban life: (1) industry, (2) education, (3) e-democracy, (4) logistics and infrastructure, (5) efficiency and sustainability, and (6) security and quality, respectively [11, 12].
This study is focused on smart mobility and examines the case of Istanbul New Airport, which officially opened on 29 October 2018. With a capacity of 200 million annual passengers and 3500 flights per day, Istanbul New Airport is the first smart airport of its size [13].
As an indicator of smart cities in terms of logistics and infrastructure, smart mobility requires urban planning that shifts the focus of transportation modes from individual to collective through the extensive use of ICT [14]. Smart mobility is concerned with local and global accessibility, ICT infrastructure, and innovative and sustainable transport systems [15]. Moreover, it should serve individuals’ needs by reducing time spent traveling and helping travelers avoid unnecessary travel altogether [16]. To provide these outputs, smart mobility should [17] accomplish the following goals:
Use technology to generate and share data, information, and knowledge that influence decisions.
Use technology to enhance vehicles, infrastructure, and services.
Derive improvements for transport system operators, users, and shareholders.
In certain situations, IT-supported service experiences can enhance customer satisfaction significantly [18]. Therefore, customer journey maps can be analyzed to observe the effects of technologies on customers’ experiences with the provided services.
Shorter life cycles make products and services more commoditized. Therefore, the differentiation has shifted from the offerings themselves to their providers that create experiences related with the acquisition, use, and maintenance of these offerings. People are naturally inclined to prefer pleasant, special experiences that have important lasting effects [19]. Thus, the opportunity for new revenue growth depends not only on driving sales of existing goods and services but on creating experiences for which customers are willing to pay [20]. Experiences can be conceptualized as “events that engage individuals in a personal way” [21] or as “enjoyable, engaging, memorable encounters for those consuming these events” [22], so creating strong customer experiences is a leading objective for management [23] to create competitive advantage [24].
Given the current progress of technology, it is possible to use it to develop customer experiences. For instance, in the fashion industry, information technologies enhance customer experiences by creating interactive and exciting shopping experiences [25]. In the banking industry, the increase of the Internet services and automated teller machines (ATMs) in various locations provides more services and more comfortable customer experiences than before [26]. In addition to B2C context, technology is used also to create B2B customer experiences, such as salespeople’s use of information technology [27].
In addition to enhancing experiences, technology advancement also provides multiple ways for customers to interact with product and service providers. These interactions are crucial to creating superior customer experiences [28]. To depict the events through which customers may interact with a service organization, academics and practitioners use a strategic management tool called customer journey mapping (CJM) [29].
Cities are considered smart when “investments in human and social capital and traditional (transport) and modern (ICT) communication infrastructure fuel sustainable economic growth and a high quality of life, with a wise management of natural resources, through participatory governance” [30]. As a dimension of smart city planning, smart mobility is considered in this study. Smart mobility can be summarized as planning and controlling transport systems through the extensive use of ICT. This kind of system has recently been applied in the building of Istanbul New Airport.
Airport information systems are divided into seven sections [31]:
Flight planning and operation
Passenger process
Business administration
Security
Facility management
Business center and airport management
Contact and information
Recently, airports in the Middle East and in Istanbul have begun to compete with European airports to create a “global hub” for connecting (transfer) passengers [32]. With the increased capacity and technologies developed at Istanbul New Airport, an improved customer experience would provide a competitive advantage. Thus, CJM is proposed in this study to depict customer experiences based on the technologies adapted at Istanbul New Airport.
The format used by Rosenbaum et al. was considered when creating the CJM [29]. On the CJM’s horizontal axis, the customer touch points take place according to a process timeline. The timeline is also divided into three periods: pre-service, service, and post-service. The pre-service period refers to customer experiences that occur before a service begins. The service period refers to customer experiences during the actual service. Finally, the post-service period refers to customer experiences occurring after the service [29]. In parallel with this process, a CJM can represent customer experiences prior to going to the airport, at the airport, and after leaving the airport, respectively.
To develop a CJM for Istanbul New Airport, customer touch points are determined first to build the CJM’s horizontal axis. The general limitation of CJM indicated by Rosenbaum et al. was that a common underlying assumption for customer touch points was the consideration that each touch point was equally important to the planning process; however, not all customers experience all touch points [29]. Thus, 62 students with previous flight experiences were recruited from two undergraduate marketing classes at Marmara University using a convenience sampling method. As the Istanbul New Airport was not operating at full capacity at the time of the study, the selection criterion was limited to participants’ previous flight experience at other airports in Istanbul (Istanbul Atatürk Airport or Istanbul Sabiha Gökçen Airport). To determine a unique CJM, only flights departing from the airports were considered. The main assumption for this approach was that passengers spend more time—or, in other words, they experience more—at the departure airport.
As discussed previously, the main assumption of CJM is that each passenger’s touch points are considered to be of equal importance. To address this limitation, the students were asked to indicate the first touch points that came to mind regarding the departure airports in Istanbul. As they all experienced different touch points, all the steps gathered from the students are listed in Table 1 to create a complete list of customer journey touch points. The percentages of listed touch points are indicated next to them. At the end of this step, a total of 33 touch points was identified by the respondents. Of the steps, 7 occurred during the pre-service period (before passengers arrive to the airport), 20 occurred during the service period (when passengers are at the airport), and 6 occurred during the post-service period (after passengers leave the airport). After the collection of the touch points for Istanbul Airport as a departure airport, two marketing professors from Marmara University checked them for a potential missing point.
(% listed) | |
---|---|
Pre-service period (before passengers arrive at the airport) | |
Please list your pre-service (before going to the airport) touch points with the airport (such as “seeing an advertisement on a street billboard about the airport”) | |
1. Preparing luggage | 1.61 |
2. Buying tickets (online or through agencies) | 37.10 |
3. Transportation (public or private) to the airport | 41.94 |
4. Checking in online | 9.68 |
5. Visiting the airport’s website or mobile application | 9.68 |
6. Searching for information about facilities at the airport | 1.61 |
7. Seeing advertising (on a street billboard, a website, or a social media service) about the airport | 40.32 |
Service period (when passengers are at the airport) | |
Please list your during-service (when you are at the airport) touch points with the airport (such as “using the parking lot of the airport”) | |
1. Using the parking lot | 16.13 |
2. Security screening process | 9.68 |
3. Checking in at the airport | 19.35 |
4. Delivering luggage | 8.06 |
5. Asking for help from airport personnel (such as asking for general information or for a wheelchair) | 1.61 |
6. Eating or drinking in the cafés at the airport (including smoking rooms) | 56.45 |
7. Using an ATM to withdraw money | 1.61 |
8. Exchanging money | 1.61 |
9. Using lounge services | 9.68 |
10. Using the toilets | 9.68 |
11. Shopping at the airport | 11.29 |
12. Paying for stamp fees | 3.23 |
13. Passport control | 0 |
14. Tracking flight gates on the screens | 1.61 |
15. Going to flight gates | 4.84 |
16. Visiting duty-free stores | 11.29 |
17. Waiting in the waiting areas (such as reading a book or listening to music) | 16.13 |
18. Connecting to Wi-Fi | 8.06 |
19. Taking photos in the airport | 1.61 |
20. Boarding | 3.23 |
Post-service period (after passengers leave the airport) | |
Please list your after service (when you leave the airport) touch points with the airport (such as “talking to friends or family about the airport”) | |
1. Baggage collection (at the destination airport) | 9.68 |
2. Calling (informing) family about arrival | 12.90 |
3. Talking to friends or family about experiences at the airport | 48.39 |
4. Communicating with the airport post-services (completing a survey about experiences at the airport) | 3.23 |
5. Writing about the airport on the Internet | 1.61 |
6. Sharing photos taken at the airport on social media | 1.61 |
Istanbul New Airport’s key horizontal axis customer touch points.
The vertical axis for CJM reflects the managerial practices that enable passengers to experience each touch point in a satisfactory way [29]. As the purpose of this study is to reveal customer experiences with technology applications, only the corresponding technological application is considered regarding passenger touch points at Istanbul New Airport.
Turkish Airlines’ move from Istanbul Atatürk Airport to the Istanbul New Airport coincides with the time of this study (5–7 April 2019), so it was not possible to meet with authorities at Istanbul New Airport. However, secondary data were used to list the corresponding technological applications. A meeting was held with Ms. Hülya Zerener Gürbaşak, the corporate account manager of Technopc, which provides more than 4000 hardware products to Istanbul New Airport. These products include desktop, mini, integrated, industrial, and kiosk computers used at check-in, security, card access, and passport control points. In addition, Mr. Mertcan Tanaydı, the communication chief of İGA Istanbul Airport, provided several documents and a video [33] in which the technologies of the airport are explained in detail from a customer’s point of view.
In terms of technological infrastructure at Istanbul New Airport, three data centers support artificial intelligence (AI) and smart systems. There are 647 servers, 3267 flight displays, 4549 computers, and more than 3000 card access points. To integrate these systems, 1740 km fiber and 4500 km copper cables were used. Data from all systems can reach up to 209 million GB. A total of 708 employees works in technology support roles [33].
The main focus of the technology was a mobile application developed to assist passengers. The airport mobile application can be used before, during, and after service. It guides passengers from home to the airport, assisting with time management by considering the traffic on the road (corresponding to the pre-service touch point). Its “Where is my car?” service also helps passengers find their cars in the parking lot among 19,000 cars in the closed area and 40,000 cars in the open area (corresponding to the post-service touch point). All corresponding technological applications for the service period are listed in Table 2.
Passenger touch points during the service period | Corresponding technological applications |
---|---|
1. Using the parking lot | A total of 4500 cameras tracks the cars in the parking lot; they take photos of the cars and upload them on the airport mobile application. Visitors may find their cars by writing their license plate on the application |
2. To be controlled by security | Electronic screens at the airport entrance show wait times at the security points (based on sensors and cameras that produce heat maps showing the density of people). Accordingly, the number of security points increases or decreases. In addition, the security cameras with AI use facial recognition systems and warn security if they detect unfavorable movements in the airport |
3. Checking in at the airport | Self-check-in points allow passengers to check in for their flights and leave their luggage |
4. Delivering luggage | |
5. Asking airport personnel for help (asking for general information or for a wheelchair) | An interactive passenger assistant located at the airport enables passengers to connect to customer service and make a video call with a responsible party who can see the passenger’s flight details; the customer opens the e-ticket’s QR code and puts the mobile phone to the device. The cameras and sensors on the top scan the e-ticket’s QR code, enabling the responsible party to see both the passenger and the ticket. In this way, the responsible party can generate a personal map for the passenger from the current location to the flight gate |
6. Eating and drinking in the cafés at the airport (including lounge services and smoking rooms) | The airport location guide provided by the airport mobile application lists all facilities and stores at the airport |
7. Using an ATM to withdraw money | |
8. Exchanging money | |
9. Using lounge services | |
10. Using the toilets | |
11. Shopping at the airport | |
12. Paying for stamp fees | |
13. Passport control | The iGate-fast passport control system includes two steps. The first door is opened when the passport is scanned by a device, and the second door is opened when a passenger’s face and hand are scanned by a device and matched to the passport |
14. Tracking flight gates on screens | Flight information screens and the airport mobile application provide flight information |
15. Going to flight gates | Personalized direction is provided by the airport mobile application to the gate for the selected destination |
16. Visiting duty-free stores | Pre-ordering is available in duty-free stores, where salespeople can reserve passengers’ pre-ordered items |
17. Waiting in the waiting areas (reading a book and listening to music) | USB inputs between the seats enable passengers to charge their mobile devices |
18. Connecting to Wi-Fi | Up to 1 h of free Wi-Fi is available at the airport |
19. Taking photos in the airport | |
20. Boarding | Boarding time can be seen in the airport mobile application |
Corresponding technological applications during the service period at Istanbul New Airport.
In addition to existing technologies, new ones are planned for the airport. There will be a store offering inventions and technological products where visitors may have such experiences as flying a drone. Moreover, three types of robots will work in the airport. Service robots will assist passengers and will reply to their questions about such topics as flight gates and ticket offices. The other robots will be responsible for cleaning and safety. They will be called “İGAbots.” Another innovation will be autonomous vehicles, which will be called “İGAbus.” They will carry passengers to various places at the airport [33].
City governments today must manage increasing urban populations in smart ways. In other words, large amounts of data produced by the population should be used to create sustainable places by decreasing the chaos of overcrowding, such as traffic, pollution, and waste. One smart city dimension is smart mobility, which refers to enhancing individuals’ mobility using innovation and technology. Technology is also essential to creating customer experiences. CJM can be used to analyze touch points and their corresponding created experiences.
In this study, an attempt was made to use CJM as a tool to analyze Istanbul New Airport, one of the largest smart airports in the world, which promises memorable customer experiences. In this way, Istanbul New Airport aims to compete with other airports defined as hubs in Europe. Therefore, a customer journey was created based on a survey of 62 undergraduate students who were asked which touch points came to mind first. The corresponding technologies were indicated based on secondary data.
According to the results, the most indicated touch point from the participants was “talking to friends or family about experiences at the airport” (48.39%). However, the question should be considered to evaluate this high rate. To make the questions clear and to get more touch points, an example was provided for pre-service, service, and post-service periods. Therefore, these three questions were recalls rather than the points coming to the respondents’ minds first. Nevertheless, the findings provide evidence that touch points do not have equal importance for all passengers. Different passengers experience different touch points during their journeys, so they perceive different experiences with the technological applications.
As can be seen from the touch point-technology match, Istanbul New Airport provides experiences through technological applications for most passenger touch points. Of these technologies, the main focus is on the mobile application created to affect various points of a customer journey, including time management and considering the traffic on the road to the airport, car location in the parking lot, guides listing all the facilities and stores in the airport, flight information for the selected destination, and personalized directions to the flight gate. In addition, various technologies are used to enhance passenger experiences, such as self-check-in points, interactive passenger assistants, AI-integrated security cameras, fast passport control system, and free Wi-Fi. According to the CJM, customer experience creators should also consider passengers’ use of social media and create a strategy accordingly. Passengers like to take photos at the airport and share them on their social media accounts, so there may be several photo opportunities when they experience a new technology. In this way, passengers may share and transfer their experiences with their surroundings, leading to positive word-of-mouth communication about the airport.
Regarding the limitations of this study, as the airport was not running at full capacity, the CJM was created based on participants’ experiences at other airports in Istanbul. Therefore, a new CJM should be created after the airport begins to run at full capacity by considering the airport from both departure and arrival perspectives to extend customers’ experiences. In addition to technological applications, other managerial practices can be also included in the CJM’s vertical axis.
IntechOpen implements a robust policy to minimize and deal with instances of fraud or misconduct. As part of our general commitment to transparency and openness, and in order to maintain high scientific standards, we have a well-defined editorial policy regarding Retractions and Corrections.
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\\n\\nA Statement of Concern detailing alleged misconduct will be issued by the Academic Editor or publisher following a 3rd party report of scientific misconduct when:
\\n\\nIntechOpen believes that the number of occasions on which a Statement of Concern is issued will be very few in number. In all cases when such a decision has been taken by the Academic Editor the decision will be reviewed by another editor to whom the author can make representations.
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\\n\\nA Correction will be issued by the Academic Editor when:
\\n\\n3.1. ERRATUM
\\n\\nAn Erratum will be issued by the Academic Editor when it is determined that a mistake in a Chapter originates from the production process handled by the publisher.
\\n\\nA published Erratum will adhere to the Retraction Notice publishing guidelines outlined above.
\\n\\n3.2. CORRIGENDUM
\\n\\nA Corrigendum will be issued by the Academic Editor when it is determined that a mistake in a Chapter is a result of an Author’s miscalculation or oversight. A published Corrigendum will adhere to the Retraction Notice publishing guidelines outlined above.
\\n\\n4. FINAL REMARKS
\\n\\nIntechOpen wishes to emphasize that the final decision on whether a Retraction, Statement of Concern, or a Correction will be issued rests with the Academic Editor. The publisher is obliged to act upon any reports of scientific misconduct in its publications and to make a reasonable effort to facilitate any subsequent investigation of such claims.
\\n\\nIn the case of Retraction or removal of the Work, the publisher will be under no obligation to refund the APC.
\\n\\nThe general principles set out above apply to Retractions and Corrections issued in all IntechOpen publications.
\\n\\nAny suggestions or comments on this Policy are welcome and may be sent to permissions@intechopen.com.
\\n\\nPolicy last updated: 2017-09-11
\\n"}]'},components:[{type:"htmlEditorComponent",content:'IntechOpen’s Retraction and Correction Policy has been developed in accordance with the Committee on Publication Ethics (COPE) publication guidelines relating to scientific misconduct and research ethics:
\n\n1. RETRACTIONS
\n\nA Retraction of a Chapter will be issued by the Academic Editor, either following an Author’s request to do so or when there is a 3rd party report of scientific misconduct. Upon receipt of a report by a 3rd party, the Academic Editor will investigate any allegations of scientific misconduct, working in cooperation with the Author(s) and their institution(s).
\n\nA formal Retraction will be issued when there is clear and conclusive evidence of any of the following:
\n\nPublishing of a Retraction Notice will adhere to the following guidelines:
\n\n1.2. REMOVALS AND CANCELLATIONS
\n\n2. STATEMENTS OF CONCERN
\n\nA Statement of Concern detailing alleged misconduct will be issued by the Academic Editor or publisher following a 3rd party report of scientific misconduct when:
\n\nIntechOpen believes that the number of occasions on which a Statement of Concern is issued will be very few in number. In all cases when such a decision has been taken by the Academic Editor the decision will be reviewed by another editor to whom the author can make representations.
\n\n3. CORRECTIONS
\n\nA Correction will be issued by the Academic Editor when:
\n\n3.1. ERRATUM
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\n\n3.2. CORRIGENDUM
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\n\n4. FINAL REMARKS
\n\nIntechOpen wishes to emphasize that the final decision on whether a Retraction, Statement of Concern, or a Correction will be issued rests with the Academic Editor. The publisher is obliged to act upon any reports of scientific misconduct in its publications and to make a reasonable effort to facilitate any subsequent investigation of such claims.
\n\nIn the case of Retraction or removal of the Work, the publisher will be under no obligation to refund the APC.
\n\nThe general principles set out above apply to Retractions and Corrections issued in all IntechOpen publications.
\n\nAny suggestions or comments on this Policy are welcome and may be sent to permissions@intechopen.com.
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