Neisseria adhesin A (NadA) (NadA)

Neisseria adhesin A (NadA) is a surface-exposed trimeric autotransporter adhesin (TAA) found in Neisseria meningitidis, primarily associated with hypervirulent serogroup B lineages (UniProt P0C1S8). It plays a pivotal role in bacterial pathogenesis by facilitating adhesion to and invasion of human epithelial and endothelial cells (PubMed: 12192019). NadA achieves this by interacting with host receptors, most notably the lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1) (PubMed: 19458284). In the context of immunization, NadA is a key antigen in the 4CMenB vaccine (Bexsero), where it elicits high titers of bactericidal antibodies (PubMed: 23078801). These vaccine-elicited antibodies target the NadA head domain, neutralizing its adhesive properties and promoting complement-mediated killing of the pathogen (PubMed: 25135623). The protein's structure consists of a distal head domain for binding, a coiled-coil stalk, and a C-terminal membrane anchor (PubMed: 16412484). Understanding the interaction between NadA and vaccine-elicited antibodies is crucial for assessing vaccine breadth and the potential for bacterial escape through antigenic variation (PubMed: 20605231).

Other names

NadAMeningococcal adhesin AAdhesin ANMB1994

Vaccine-elicited antibodies bind to the extracellular domain of NadA, preventing bacterial attachment to host cells and activating the classical complement pathway to induce lysis (PubMed: 23078801).