Streptococcus agalactiae surface protein (GBS surface protein)

Streptococcus agalactiae surface proteins are a diverse group of cell-wall-anchored polypeptides that play fundamental roles in the virulence and colonization of Group B Streptococcus (GBS) (UniProt P0A4L9, P13515) [1, 2]. These proteins, which include the Alpha-like protein (Alp) family, C5a peptidase (ScpB), and various pili, are essential for adhering to host extracellular matrix components and evading the host immune system (PubMed: 23935143) [3]. For example, the Rib and Alpha C proteins are involved in epithelial cell invasion, while ScpB degrades host C5a to prevent neutrophil recruitment (PubMed: 31401100) [4]. Due to their high exposure on the bacterial surface and relative conservation across different serotypes, these proteins are primary targets for the development of maternal vaccines (Minervax) [5]. The therapeutic strategy involves immunizing pregnant women to generate high levels of IgG antibodies, which are then transferred to the fetus to prevent neonatal sepsis and meningitis [4, 5]. Current clinical candidates, such as the GBS-NN vaccine, utilize recombinant fusion proteins of these surface antigens to provide broad protection against GBS infections [5].

Other names

Group B Streptococcus surface proteinAlpha-like proteinAlp familySurface protein RibAlpha C proteinC5a peptidaseScpBPili proteinsLaminin-binding protein

Induction of opsonophagocytic antibodies that facilitate bacterial clearance and provide passive immunity to neonates via transplacental transfer.