Neisseria meningitidis serogroup B factor H binding protein (Subfamily A05) (fHbp)

Neisseria meningitidis serogroup B factor H binding protein (fHbp) is a surface-exposed lipoprotein that plays a crucial role in the survival of the bacterium within the human host (UniProt Q9K0U4). Its primary function is to bind human factor H, a negative regulator of the alternative complement pathway, which enables the pathogen to evade complement-mediated killing (PubMed: 19126564). By mimicking host cells through the recruitment of factor H, the bacteria prevent the deposition of C3b on their surface. fHbp is a key component of modern protein-based vaccines against serogroup B meningococcal disease, such as Trumenba and Bexsero (FDA Trumenba Label). The protein is highly diverse and is classified into two main subfamilies, A and B; subfamily A05 is a specific variant included in bivalent vaccine formulations like Trumenba to ensure broad coverage against circulating strains (PubMed: 25344445). Therapeutic intervention via vaccination induces the production of bactericidal antibodies that target fHbp, leading to bacterial lysis and neutralizing the protein's ability to bind factor H.

Other names

Factor H-binding proteinfHbpGNA1870LP2086Lipoprotein 2086Genome-derived Neisserial Antigen 1870rLP2086

Induction of complement-mediated bactericidal antibodies that target the fHbp protein on the surface of Neisseria meningitidis, thereby facilitating bacterial lysis and preventing immune evasion by blocking factor H binding (FDA Trumenba Label; PubMed: 25344445).