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B-cell receptors (BCRs) specific for the polyribosyl ribitol phosphate (PRP) epitopes of Haemophilus influenzae type b (Hib) are membrane-bound immunoglobulins that play a central role in the immune recognition of this pathogen (Kelly et al., 2004). PRP is the primary capsular polysaccharide and a major virulence factor of Hib, which causes severe infections such as meningitis and pneumonia, particularly in children (WHO, 2019). These BCRs recognize and bind to the repeating units of PRP, initiating signal transduction pathways that lead to B-cell activation and differentiation. In modern vaccinology, Hib conjugate vaccines are designed to target these BCRs by linking the PRP polysaccharide to a carrier protein, thereby converting a T-cell independent response into a T-cell dependent one (Pichichero, 2013). This interaction is essential for the generation of high-affinity IgG antibodies and long-lived memory B cells, which provide durable protection against Hib-related diseases (CDC, 2022). Monitoring the activity and frequency of these specific BCRs and the resulting antibody titers serves as a primary measure of vaccine efficacy.
Antigen-mediated B-cell receptor cross-linking and activation leading to clonal expansion, T-cell dependent maturation (for conjugates), and secretion of anti-PRP antibodies (Pichichero, 2013; CDC, 2022).
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