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Beta-galactosidase BgaA is a large, multifunctional surface-associated enzyme primarily found in Streptococcus pneumoniae. It belongs to the glycosyl hydrolase family 2 and plays a critical role in bacterial pathogenesis by sequentially deglycosylating host glycoconjugates, such as those found in human mucus and cell surfaces, to provide carbon sources for bacterial growth. Beyond its enzymatic activity, BgaA contains non-catalytic carbohydrate-binding modules that function as adhesins, mediating the attachment of the bacterium to human epithelial and endothelial cells. Furthermore, BgaA contributes to immune evasion by inhibiting the deposition of complement component C3 on the bacterial surface, thereby reducing opsonophagocytic killing by host neutrophils. Due to its essential roles in colonization, nutrient acquisition, and virulence, BgaA is considered an attractive target for the development of novel antibiotics and structure-based vaccines against pneumococcal infections.
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