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Neisseria meningitidis group B capsular and surface antigens are a collection of molecules on the surface of serogroup B meningococci, which are major causes of bacterial meningitis and sepsis [1, 3]. The group B capsule is unique among meningococci because it consists of α(2→8)-linked polysialic acid, a structure that mimics human neural cell adhesion molecules (NCAM) [4, 6]. This molecular mimicry results in poor immunogenicity and has historically hindered the development of traditional polysaccharide-based vaccines due to potential autoimmune risks [1, 16]. Consequently, modern therapeutic strategies focus on sub-capsular surface proteins, including Factor H binding protein (fHbp), Neisserial adhesin A (NadA), and Neisserial Heparin Binding Antigen (NHBA) [5, 9]. These antigens are essential for the bacterium's pathogenesis, facilitating host cell adhesion and evasion of the alternative complement pathway [9, 17]. Vaccines targeting these antigens, such as Bexsero and Trumenba, work by eliciting serum bactericidal antibodies that promote complement-mediated lysis and opsonophagocytosis [11, 14, 15]. Clinical efficacy is typically monitored using serum bactericidal antibody (SBA) titers, which serve as a correlate of protection [9, 14]. Challenges in targeting these antigens include the high genetic diversity of MenB strains, which can lead to variable vaccine coverage across different geographic regions [8, 10].
Induction of bactericidal antibodies that facilitate complement-mediated killing and opsonophagocytosis of Neisseria meningitidis serogroup B [11, 14, 15].
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