Neisseria meningitidis factor H binding protein subfamily B (fHbp subfamily B)

Neisseria meningitidis factor H binding protein (fHbp) is a critical surface-exposed lipoprotein that enables the bacterium to evade the human innate immune system. It functions by specifically binding to human Factor H, a negative regulator of the alternative complement pathway, thereby protecting the meningococci from complement-mediated lysis and opsonophagocytosis [1, 2]. fHbp is categorized into two distinct subfamilies, A and B (also known as variant groups 2/3 and 1, respectively), which show significant sequence diversity and limited immunological cross-reactivity [3]. Subfamily B variants are highly prevalent among clinical isolates of serogroup B Neisseria meningitidis and serve as a primary component of modern protein-based vaccines [4]. By including fHbp subfamily B variants in vaccine formulations, the immune system is trained to produce serum bactericidal antibodies that block Factor H binding and facilitate bacterial killing [5]. This target is essential for providing broad protection against the diverse strains of MenB that cause life-threatening meningitis and septicemia [6]. Sources: [1] UniProt (P0C1S8 - FHBP_NEIMB) [2] Schneider et al. (2009) Nature, PMID: 19181964 [3] Fletcher et al. (2004) Infection and Immunity, PMID: 15105504 [4] FDA Prescribing Information for Trumenba and Bexsero [5] Pajon et al. (2011) Vaccine, PMID: 21844305 [6] CDC Meningococcal Disease Clinical Information

Other names

Factor H binding protein variant group 1fHbp variant 1GNA1870LP2086Genome-derived Neisseria Antigen 1870Lipoprotein 2086

Induction of complement-mediated serum bactericidal antibodies that target the protein and inhibit its interaction with human Factor H.