Chapters authored
Cell Surface and Cytosolic Proteins of Group B Streptococcus Adding New Dimensions in Its Colonization and Pathogenesis
Streptococcus agalactiae or Group B streptococcus (GBS) is an opportunistic human pathogen known for their invasive diseases caused in newborns, pregnant women, and nonpregnant adults. This pathogen even being an asymptomatic colonizer of adult humans, still they result in a broad range of disease manifestations starting from mild skin diseases to pneumonia, meningitis, and septicemia. Of the 10 GBS capsular types, the majority of invasive neonatal diseases are associated with the serotype III. GBS is a pathogen that has developed some strategies to resist host immune defenses. The formidable array of GBS virulence factors makes this bacterium at the forefront of neonatal pathogens. The involvement of bacterial components in the host-pathogen interaction of GBS pathogenesis and its related diseases is thought to be due to a variety of virulence factors expressed by Streptococcus agalactiae. Pathogenic factors of streptococcus promote infections by their coordinated activity. These factors/determinants initially get a stimulus by the communication between specific ligands and their respective receptors in a host-pathogen interaction. These in turn activate adhesion and invasion mechanisms by mediating the attachment of pathogen via cell wall associated/secretory proteins, e.g., adhesins followed by their entry into the host cell eventually deciding their fate to live by activation of mechanisms like phagocytosis. These mediators/determinants also modulate the immune responses by the host toward the pathogen. A number of new GBS surface-exposed or secreted proteins have been identified (GBS immunogenic bacterial adhesion protein, leucine-rich repeat of GBS, serine-rich repeat proteins), the three-dimensional structures of known streptococcal proteins (αC protein, C5a peptidase) have been solved, and an understanding of the pathogenetic role of “old” and new determinants has been better defined in recent years. Recently, a 39kDa Invasion Inhibitory Factor (IIF) was isolated from GBS playing an important role in its invasion. A homogeneous non-toxic 39 kDa factor from the cytosol of GBS showing a homology with xenobiotic response element type transcriptional regulator protein adds another quill to the GBS protein panama, thus indicating that such protein molecules can be efficiently explored as suitable vaccine candidates. These observations add a novel aspect to bacterial pathogenesis where bacteria’s own intracellular protein component can act as a potential therapeutic candidate by decreasing the severity of disease thus promoting its invasion inhibition.
Part of the book: Staphylococcus and Streptococcus