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Description

Factor H-binding protein (UniProt: Q6QCC2, also known as Lipoprotein, Lipoprotein GNA1870) is encoded by the gna1870 (also known as fhbp) gene (Gene ID: 2827909) in Neisseria meningitidis. Neisseria meningitidis, an encapsulated Gram-negative bacterium, is an important cause of bacterial sepsis and meningitis. FHbp, a surface exposed lipoprotein, is present in all strains of Neisseria meningitidis but is usually sparsely expressed. It is reported to be the major receptor for human Factor H (FH), a down-regulatory protein of the alternate complement pathway. Recruitment of FH is the major contributory factor to the ability of this bacteria to avoid innate immune response via inhibition of complement-mediated lysis. High affinity between human FH and FHbp is reported to be responsible for sequestering FH in the plasma and down-regulation of the complement system, which in the absence of down-regulation can cause complement-mediated damage to the bacteria. FHbp exists in two major antigenic sub-families known as A and B that do display minimal cross-protective activity. FHbp also has been divided into three variant groups based on its amino acid sequence. Variant group 1 belongs to subfamily B and accounts for about 60% of disease-causing serogroup B isolates. Subfamily A includes variant groups 2 and 3. Antibodies generated against variant 1 are reported to be bactericidal only against bacterial strains expressing FHbp in the variant 1 group but not against strains that express variants 2 and 3 and vice versa. Clone JAR1 is shown to react with an epitope expressed only by ET5 complex strain MC58. It is shown to confer protection against strain NZ98/254. (Ref.: Vu, DM et al., (2012). Sci. Rep. 2: 341, Beernink, PT et al., (2009). Mol. Immunol. 46(8-9), 1647-1653, Welsch, JA., et al. (2004). J. Immunol. 172(9), 5606-5615).