B cell receptor specific for Neisseria meningitidis group C capsular polysaccharide (MenC-specific BCR)

The B cell receptor specific for Neisseria meningitidis group C capsular polysaccharide is a membrane-bound immunoglobulin molecule located on the surface of specific B lymphocytes (Pollard et al., 2001, Lancet). Its primary biological function is the recognition and binding of the α2-9-linked sialic acid polymer that constitutes the MenC capsule, a critical virulence factor (Frasch et al., 2005, Vaccine). Upon binding, the receptor initiates intracellular signaling pathways that lead to B cell activation, proliferation, and differentiation into antibody-secreting plasma cells (Goldblatt, 2000, J. Med. Microbiol.). In the context of vaccination, this receptor is the primary target for conjugate vaccines, which link the polysaccharide to a carrier protein to recruit T-cell help (Borrow et al., 2001, Epidemiology and Infection). This interaction is essential for preventing invasive meningococcal disease, including meningitis and sepsis, by generating protective bactericidal antibodies (Richmond et al., 1999, Lancet). Therapeutic engagement of this receptor via vaccination has significantly reduced the incidence of MenC-related morbidity and mortality worldwide (Ramsay et al., 2001, BMJ).

Other names

MenC BCRNeisseria meningitidis serogroup C capsular polysaccharide-specific B cell receptorAnti-MenC B-cell receptor

The target acts as the primary recognition site for the MenC polysaccharide antigen; binding triggers B cell activation, internalization of the antigen-carrier complex, and subsequent presentation to T cells, leading to high-affinity antibody production and immunological memory (Goldblatt, 2000).