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Factor H binding protein (fHbp) is a surface-exposed lipoprotein essential for the survival of Neisseria meningitidis in human blood. Its primary biological function is to bind human factor H, a key down-regulator of the alternative complement pathway, which protects the bacteria from complement-mediated lysis and opsonophagocytosis [1, 2]. By recruiting factor H to its surface, the pathogen effectively mimics host cells and evades the innate immune response [3]. fHbp is highly diverse and is categorized into two main subfamilies (A and B) or three variants (1, 2, and 3), which are critical for broad-spectrum vaccine coverage [4]. In the context of disease, fHbp is a major virulence factor for serogroup B meningococci, which are a leading cause of life-threatening meningitis and sepsis worldwide [5]. As a therapeutic target, fHbp is the primary component of recombinant protein vaccines like Trumenba and a key component of Bexsero [6]. These vaccines work by eliciting bactericidal antibodies that block factor H binding and trigger the classical complement pathway to kill the bacteria [7].
Induction of serum bactericidal antibodies that bind to fHbp on the surface of Neisseria meningitidis, preventing factor H recruitment and facilitating complement-mediated bacterial lysis.
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