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The surface proteins of Neisseria meningitidis that share epitopes with serogroup B (MenB) antigens primarily include Factor H-binding protein (fHbp), Neisserial Heparin Binding Antigen (NHBA), and Neisserial adhesin A (NadA). These proteins are essential for the survival and pathogenesis of the bacteria, facilitating functions such as adhesion to host cells and evasion of the host innate immune system (Pizza et al., 2000). For example, fHbp binds to human Factor H to inhibit the alternative complement pathway, protecting the bacteria from lysis (Serruto et al., 2012). While originally identified as targets for MenB vaccines, these proteins are also expressed by non-B serogroups (A, C, W, Y, and X), allowing for broad-spectrum cross-protection (Ladhani et al., 2016). Vaccines targeting these antigens work by eliciting bactericidal antibodies that recognize the proteins on the bacterial surface, triggering complement-mediated destruction. This cross-reactivity is a key strategy in developing universal meningococcal vaccines that can address multiple serogroups simultaneously (Jiang et al., 2010).
Induction of serum bactericidal antibodies that recognize conserved surface proteins, leading to complement-mediated killing and opsonophagocytosis of the bacteria across multiple serogroups.
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