Neisseria meningitidis antigen (None (specific antigens have accepted abbreviations, see aliases))

"Neisseria meningitidis antigen" is not a single molecule but refers to a set of structurally and functionally diverse molecules found on the surface of the Gram-negative bacterium Neisseria meningitidis. The main antigens that have been established as targets for vaccine development and as mediators of pathogenicity include: factor H binding protein (fHbp), which allows the bacterium to evade complement-mediated killing by binding human complement factor H; Neisseria adhesin A (NadA), a trimeric autotransporter involved in adhesion and invasion of host cells; Neisseria heparin binding antigen (NHBA), which enhances serum resistance via binding to heparin/heparan sulfate and promotes adherence and biofilm formation; PorA, an immunodominant porin frequently targeted by vaccine-induced antibodies; and the capsule polysaccharide, the main distinguishing antigen for serogrouping the pathogen. These antigens are core components of current vaccines, such as Bexsero, designed to prevent invasive meningococcal disease. They act as immunogens to stimulate protective antibody responses. Antigenic and phase variation, however, can limit the breadth of protection, and some antigenic targets (like LOS) are associated with severe inflammatory responses. The term "Neisseria meningitidis antigens" is too broad for a truly canonical molecular target name and should, wherever possible, be replaced with singular, specific antigen names in data structures or when discussing molecular targets.

Other names

Meningococcal antigensMeningococcal surface antigensNeisseria meningitidis surface antigensSpecific well-studied examples:Factor H binding protein (fHbp)Neisseria adhesin A (NadA)Neisseria heparin binding antigen (NHBA)Porin A (PorA)Lipooligosaccharide (LOS)

Induction of bactericidal antibodies by vaccination Blocking bacterial adhesion/invasion by targeting adhesins (NadA, NHBA) Inhibition of complement factor binding (fHbp)