Human B-cell receptor recognizing pneumococcal capsular polysaccharide epitopes (BCR-PPS)

The Human B-cell receptor (BCR) recognizing pneumococcal capsular polysaccharide (PPS) epitopes is a specialized transmembrane protein complex on the surface of B lymphocytes. Its primary biological function is the specific recognition and binding of the complex carbohydrate structures that form the protective capsule of Streptococcus pneumoniae (1). Upon binding these epitopes, the receptor initiates intracellular signaling cascades, involving molecules like Syk and PLC-gamma2, which drive the expansion of specific B-cell clones and their maturation into antibody-secreting plasma cells (2). This process is critical for the humoral immune defense against invasive pneumococcal diseases such as pneumonia, meningitis, and sepsis (3). In clinical practice, this receptor is the primary physiological target for pneumococcal vaccines, such as PCV13 and PPSV23, which provide purified or conjugated polysaccharides to stimulate the production of protective opsonizing antibodies (4). Understanding the repertoire and affinity of these receptors is essential for developing more effective vaccines that cover a broader range of bacterial serotypes and provide long-lasting immunity (5). Sources: (1) PubMed PMID: 25108491; (2) ScienceDirect, 'The B-cell receptor: from basic biology to clinical strategy'; (3) Nature Reviews Microbiology, 'Streptococcus pneumoniae: Transmission, Colonization and Invasion'; (4) CDC, 'Pneumococcal Vaccination Guide'; (5) Journal of Immunology, 'Molecular analysis of the human B cell response to Streptococcus pneumoniae'.

Other names

Pneumococcal polysaccharide-specific B-cell receptorAnti-PPS BCRStreptococcus pneumoniae capsular polysaccharide B-cell receptorPPS-specific BCR

Binding of pneumococcal capsular polysaccharide antigens to the B-cell receptor triggers receptor cross-linking and intracellular signaling, leading to B-cell proliferation and differentiation into antibody-secreting plasma cells.