Group B Streptococcus Alpha-like protein family N-terminal domains (GBS Alp N-terminal domains)

The Group B Streptococcus (GBS) Alpha-like protein (Alp) family consists of several large, surface-anchored proteins, including Alpha C, Rib, Alp1, Alp2, Alp3, and Alp4 (Lindahl et al., 2005). These proteins are characterized by a conserved N-terminal domain and a variable number of tandem repeats, playing a crucial role in GBS virulence by mediating adhesion to host epithelial cells and facilitating immune evasion (Bolduc et al., 2002). The N-terminal domains are highly immunogenic and surface-exposed, making them primary targets for vaccine development aimed at preventing invasive GBS disease in neonates (Fischer et al., 2021). Therapeutic strategies, such as the GBS-NN vaccine candidate, utilize recombinant N-terminal domains to induce high titers of protective opsonophagocytic antibodies (Minervax, 2023). These antibodies bind to the bacterial surface, promoting phagocytosis and clearance by host immune cells, thereby providing broad protection against various GBS serotypes that express Alp family proteins (Donders et al., 2016).

Other names

Alp family proteinsAlpha-like proteinsRib proteinAlpha C proteinAlp1Alp2Alp3Alp4GBS surface proteins

Induction of opsonophagocytic antibodies that bind to the N-terminal domains of Alp proteins on the bacterial surface, facilitating phagocytosis and clearance by immune cells.