Human B-cell receptor recognizing Streptococcus pneumoniae serotype 23F capsular polysaccharide epitopes

The Human B-cell receptor (BCR) recognizing Streptococcus pneumoniae serotype 23F capsular polysaccharide epitopes is a membrane-bound immunoglobulin complex essential for the humoral immune response against pneumococcal infection (Source 1.2.2). It specifically identifies the complex carbohydrate structures of the 23F capsule, with a particular affinity for the immunodominant L-rhamnose epitope (Source 1.2.1, 1.3.1). In humans, the response to this serotype is often characterized by the use of specific immunoglobulin light chain genes, notably VkappaL6 and VkappaA23 (Source 1.3.1). Binding of the 23F polysaccharide to this BCR initiates a cascade of signal transduction that drives B-cell activation, clonal expansion, and the eventual secretion of protective IgG and IgM antibodies (Source 1.2.2). These antibodies are vital for opsonizing the encapsulated bacteria, facilitating their clearance by phagocytic cells like neutrophils and macrophages (Source 1.2.2, 1.3.5). This receptor is the functional target of several widely used vaccines, such as the 13-valent pneumococcal conjugate vaccine (PCV13) and the 23-valent pneumococcal polysaccharide vaccine (PPSV23) (Source 1.1.4, 1.3.5). By stimulating these specific BCRs, vaccines induce immunological memory, providing long-term protection against invasive diseases like pneumonia, bacteremia, and meningitis (Source 1.2.4, 1.3.5).

Other names

Anti-pneumococcal 23F B-cell receptorBCR-Spn23FVkappaL6-encoded B-cell receptorVkappaA23-encoded B-cell receptorStreptococcus pneumoniae serotype 23F-specific B-cell receptor

Antigen binding to the B-cell receptor triggers intracellular signaling, leading to B-cell activation, proliferation, and differentiation into antibody-secreting plasma cells and memory B cells.