Factor H-binding protein (fHbp) subfamily B (fHbp subfamily B)

Factor H-binding protein (fHbp) is a surface-exposed lipoprotein of Neisseria meningitidis that plays a critical role in bacterial immune evasion by binding human Factor H (fH), a down-regulator of the alternative complement pathway (Schneider et al., 2009, PubMed: 19506076). This binding prevents C3 deposition and subsequent complement-mediated lysis of the bacteria. fHbp is divided into two distinct subfamilies, A and B (also known as variants 2/3 and variant 1), which do not provide cross-protective immunity (Murphy et al., 2009, PubMed: 19433477). Subfamily B is a major component of the Serogroup B meningococcal vaccines, such as Trumenba (bivalent rLP2086) and Bexsero (4CMenB) (FDA, 2014; EMA, 2013). These vaccines work by inducing bactericidal antibodies that block fH binding and promote bacterial killing through the classical complement pathway. Monitoring fHbp expression and sequence variation is essential for assessing vaccine coverage against emerging clinical isolates (Bambini et al., 2013, PubMed: 23712321).

Other names

Variant 1 fHbpGNA1870LP2086 subfamily BLipoprotein 2086 subfamily BGenome-derived Neisserial Antigen 1870

Induction of serum bactericidal antibodies that inhibit the binding of human Factor H to the bacterial surface and activate the classical complement pathway for bacterial lysis.