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Factor H binding protein of Neisseria meningitidis (fHbp) is a surface-exposed lipoprotein and a major virulence factor that enables the bacterium to evade host immune responses by binding human complement factor H, thereby inhibiting complement activation on the bacterial surface[1][2][3][4][5]. fHbp is highly polymorphic with over 1000 known alleles and is present in almost all disease-causing N. meningitidis isolates[2][3][5]. It is the key antigen in two licensed vaccines (Bexsero and Trumenba) for the prevention of serogroup B meningococcal disease, where it induces protective, bactericidal antibodies[2][5]. The protein's expression varies between strains and impacts both the pathogen's virulence and the likelihood of vaccine-induced immunity protecting against different meningococcal strains[2][5]. The presence, sequence variant, and expression level of fHbp are important for predicting disease risk and vaccine efficacy[2][5].
Vaccines using fHbp as antigen induce production of antibodies that bind to fHbp, blocking its interaction with human factor H, enabling complement-mediated lysis of Neisseria meningitidis Direct bactericidal activity by anti-fHbp monoclonal antibodies, interfering with complement evasion Prevention of meningococcal infection by immune recognition of surface-expressed fHbp
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