B-cell receptor specific for Streptococcus pneumoniae serotype 18C capsular polysaccharide (BCR-Sp18C)

The B-cell receptor (BCR) specific for Streptococcus pneumoniae serotype 18C capsular polysaccharide is a membrane-bound immunoglobulin complex that plays a critical role in the adaptive immune system's recognition of pneumococcal pathogens (Source: Janeway's Immunobiology). Serotype 18C is a prevalent cause of invasive pneumococcal disease (IPD), including pneumonia and meningitis, especially in pediatric populations (Source: CDC, 'Pneumococcal Disease'). The BCR recognizes the specific repeating units of the 18C capsular polysaccharide, which consists of a branched pentasaccharide structure containing D-glucose, D-galactose, L-rhamnose, and N-acetyl-D-glucosamine with a glycerol phosphate substituent (Source: PubChem, CID 139561245). Upon binding to its cognate antigen—typically delivered via conjugate vaccines like Prevnar 13 or Prevnar 20—the BCR triggers intracellular signaling pathways that result in B-cell proliferation and the secretion of serotype-specific IgG antibodies (Source: Pfizer, 'Prevnar 20 Package Insert'). These antibodies are essential for opsonophagocytosis, the primary mechanism for clearing S. pneumoniae from the host (Source: WHO, 'Pneumococcal vaccines'). This receptor is a key target for immunization strategies aimed at reducing the global burden of pneumococcal infections.

Other names

Anti-pneumococcal serotype 18C B-cell receptorStreptococcus pneumoniae 18C-specific BCRSp18C-specific B-cell receptorAnti-18C BCR

The receptor functions by binding to the specific 18C capsular polysaccharide antigen, which triggers the cross-linking of BCRs and activates the Ig-alpha/Ig-beta signaling complex. This leads to B-cell proliferation, affinity maturation, and differentiation into plasma cells that secrete protective anti-18C antibodies (Source: Janeway's Immunobiology; Nature Reviews Immunology).