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Factor H binding protein (fHbp) is a surface-exposed lipoprotein found on Neisseria meningitidis, particularly serogroup B, which plays a vital role in bacterial survival within the human host. Its primary biological function is to bind human Factor H, a key regulatory protein that inhibits the alternative complement pathway, thereby protecting the bacteria from complement-mediated lysis and opsonophagocytosis (PMID: 19234461, PMID: 21149354). By recruiting Factor H to its surface, the pathogen effectively mimics host cells and evades the innate immune response (PMID: 15105504). In clinical medicine, fHbp is a major target for vaccines such as Trumenba and a component of Bexsero, which are designed to prevent invasive meningococcal disease (PMID: 25703118). These vaccines induce the production of serum bactericidal antibodies that either block the binding of Factor H or directly initiate the classical complement pathway to kill the bacteria (PMID: 29158406). Because fHbp exhibits significant sequence variability, it is classified into three main variants or two subfamilies, necessitating broad-spectrum vaccine formulations to ensure coverage against diverse clinical isolates (PMID: 19234461).
Vaccine antigen that elicits bactericidal antibodies to inhibit Factor H binding and promote complement-mediated bacterial lysis.
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