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Human adaptive immune receptors recognizing filamentous hemagglutinin (FHA) comprise the diverse repertoire of B-cell receptors (BCRs) and T-cell receptors (TCRs) that specifically bind to FHA, a primary virulence factor of Bordetella pertussis (Source: UniProt P03397). FHA is a large, secreted protein that facilitates the attachment of the bacteria to the respiratory epithelium and modulates the host immune response by interacting with various cell surface molecules, such as integrins (Source: PubMed PMID: 11544341). The activation of these adaptive receptors is the primary goal of acellular pertussis vaccines, such as DTaP and Tdap, which utilize purified FHA to induce neutralizing antibodies and protective T-cell responses (Source: CDC, Pertussis Vaccination). Upon recognition of FHA, B-cells differentiate into plasma cells secreting high-affinity antibodies that block bacterial adhesion and promote opsonophagocytosis, while T-cells provide help for B-cell maturation and coordinate cellular defenses (Source: PubMed PMID: 25643275). Understanding the specificity and longevity of these receptors is critical for addressing the global resurgence of pertussis and improving vaccine efficacy (Source: PubMed PMID: 30115698).
Vaccines containing filamentous hemagglutinin (FHA) act as exogenous antigens that are recognized by specific B-cell receptors (BCRs) and T-cell receptors (TCRs). This recognition triggers clonal expansion, affinity maturation, and the differentiation of B-cells into memory cells and antibody-secreting plasma cells, as well as the activation of CD4+ T-helper cells (Source: PubMed PMID: 25643275).
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