Meningococcal factor H-binding protein (fHbp)

Meningococcal factor H-binding protein (fHbp) is a surface-exposed lipoprotein and critical virulence factor of Neisseria meningitidis, enabling the bacterium to evade the human complement-mediated immune response by binding to human complement factor H (CFH), which downregulates the alternative complement pathway[1][2][3]. fHbp's structure consists of two β-barrels and it is expressed on the outer membrane via lipidation. Its high-affinity interaction with CFH is essential for meningococcal survival in human blood, contributing directly to invasive disease potential[1][3][4]. fHbp is highly diverse, classified into multiple variants, and is the basis for two licensed vaccines (Bexsero and Trumenba) targeting serogroup B meningococcus by inducing protective bactericidal antibodies that neutralize its function and facilitate complement-mediated killing[2][4][6]. Expression levels and sequence variability influence disease risk and vaccine coverage, making fHbp a key public health target and a principal biomarker for vaccine-mediated protection and epidemiological surveillance[4][5][6].

Other names

Factor H binding proteinfHbpGNA1870LP2086

Vaccines elicit bactericidal antibodies that bind fHbp, blocking its interaction with human factor H and restoring complement-mediated killing[2][6]. Antibody-dependent complement-mediated bacteriolysis[6].