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Outer membrane vesicle (OMV) surface epitopes of Neisseria meningitidis serogroup B are a complex array of protein and glycolipid antigens that serve as the primary targets for vaccines against meningococcal group B disease. Because the capsular polysaccharide of serogroup B is chemically identical to human neural cell adhesion molecules, it is poorly immunogenic and poses a risk of autoimmunity, leading researchers to target subcapsular antigens instead (Pollard et al., 2009). These epitopes include major outer membrane proteins such as PorA, PorB, and FetA, as well as key virulence factors like factor H binding protein (fHbp), Neisseria adhesin A (NadA), and Neisseria heparin-binding antigen (NHBA) (Bambini et al., 2013). Vaccines such as Bexsero (4CMenB) incorporate these OMV components to induce the production of serum bactericidal antibodies in the host (EMA, 2013). These antibodies recognize the surface epitopes and trigger the complement system to lyse the bacteria or facilitate their destruction by phagocytes (CDC, 2023). The diversity and antigenic variation of these surface epitopes across different MenB strains represent a significant challenge for achieving universal vaccine coverage.
Induction of bactericidal antibodies that facilitate complement-mediated lysis and opsonophagocytosis of the bacteria
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