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Group B Streptococcus C5a peptidase (ScpB) is a surface-anchored serine protease expressed by Streptococcus agalactiae, a leading cause of neonatal sepsis, meningitis, and pneumonia (UniProt Q99YV1; PMID: 11544341). The enzyme specifically cleaves the human chemoattractant C5a, a potent anaphylatoxin, at its C-terminal end, thereby preventing the recruitment and activation of neutrophils to the site of infection (PMID: 21844305). By neutralizing C5a, ScpB allows the bacteria to evade the host's innate immune response and facilitate systemic dissemination (PMID: 15608301). Due to its highly conserved nature across GBS serotypes and its critical role in virulence, ScpB is a prominent target for the development of recombinant protein vaccines (PMID: 21844305). Clinical-stage candidates, such as Pfizer's GBS6, utilize ScpB or related surface proteins to induce protective antibodies that neutralize peptidase activity and enhance bacterial clearance (ClinicalTrials.gov NCT03765073).
Induction of neutralizing antibodies that inhibit the proteolytic activity of ScpB and promote opsonophagocytosis of the bacteria.
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