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Streptococcal C5a peptidase is a conserved, cell-surface serine endopeptidase of group A and group B streptococci that specifically cleaves human complement fragment C5a at a His-Lys site, thereby eliminating a key chemotactic signal and enabling immune evasion; structurally, it is a subtilisin-like protease with an inserted protease-associated domain and three C-terminal fibronectin type III domains containing RGD motifs that contribute to adhesin/invasin functions, and it is under investigation as a vaccine antigen and as an engineered enzyme to modulate excessive C5a-driven inflammation
For therapeutics targeting this molecule: vaccine antigens eliciting anti-SCP antibodies to enhance opsonophagocytic killing and provide serotype-independent protection. For enzyme-as-therapy concepts: engineered ScpA proposed to reduce excessive C5a-driven inflammation by specific proteolysis of C5a.
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