Glyceraldehyde-3-phosphate dehydrogenase (Streptococcus agalactiae) (GAPDH)

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Streptococcus agalactiae (Group B Streptococcus) is a multifunctional "moonlighting" protein that plays a critical role in both bacterial metabolism and pathogenesis (Madureira et al., 2007, PLoS Pathogens). While its primary intracellular role is in the glycolytic pathway, where it catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate, it is also exported to the bacterial cell surface (Seifert et al., 2003, Journal of Bacteriology). On the surface, GAPDH acts as a major virulence factor by facilitating adhesion to host cells and binding to host proteins such as plasminogen and fibrinogen, which aids in tissue invasion (Terrade et al., 2015, Frontiers in Microbiology). Furthermore, GBS GAPDH has been shown to modulate the host immune response by inducing the production of immunosuppressive cytokines like IL-10, thereby promoting bacterial survival and systemic dissemination (Madureira et al., 2011, Journal of Immunology). Because of its essential metabolic role and its contribution to virulence, it is considered a potential target for novel antimicrobial strategies and vaccine development. However, the high degree of structural conservation between bacterial and human GAPDH poses a significant challenge for achieving therapeutic selectivity and avoiding off-target effects in the host.

Other names

SDHStreptococcal surface dehydrogenasePlrPlasmin receptorGAPDH-GBS

Inhibition of the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase and blocking of surface-mediated adhesion to host proteins.