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Neisseria meningitidis adhesin A (NadA) is a surface-exposed outer membrane protein belonging to the trimeric autotransporter adhesin (TAA) family (UniProt: Q9K0U9). It plays a critical role in the pathogenesis of Neisseria meningitidis by mediating the adhesion of the bacteria to human epithelial and endothelial cells, which is a prerequisite for colonization and subsequent invasion into the bloodstream (Comanducci et al., 2002). NadA is one of the key antigenic components of the multicomponent meningococcal serogroup B vaccine (4CMenB), where it elicits a robust immune response (Bexsero Summary of Product Characteristics, EMA). The protein consists of a C-terminal membrane-anchor domain, a stalk, and an N-terminal head domain that interacts with host cell receptors such as LOX-1 (Mazzon et al., 2007). Because NadA is present in approximately 50% of clinical isolates, particularly those belonging to hypervirulent lineages, it serves as an important target for vaccine-induced bactericidal antibodies. Therapeutic strategies focusing on NadA aim to prevent bacterial attachment and promote complement-mediated killing of the pathogen.
Induction of bactericidal antibodies that block bacterial adhesion to host cells and facilitate complement-mediated killing (Bexsero Summary of Product Characteristics, EMA).
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