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B-cell receptors (BCRs) specific for measles virus hemagglutinin (H) and fusion (F) proteins are membrane-bound immunoglobulins on the surface of B lymphocytes that recognize and bind to specific epitopes on the measles virus (Griffin, 2016). The H protein is responsible for viral attachment to host cell receptors, such as signaling lymphocytic activation molecule (SLAM/CD150) or Nectin-4, while the F protein mediates the fusion of the viral envelope with the host cell membrane (Moss, 2017). Recognition of these proteins by specific BCRs is the critical first step in the humoral immune response, leading to the production of neutralizing antibodies that block viral entry and spread (Janeway et al., 2001). These BCRs are the primary targets of measles vaccines, such as the MMR vaccine, which aim to elicit a robust and long-lasting population of memory B cells and plasma cells (CDC, 2021). Understanding the specific epitopes recognized by these receptors is essential for developing next-generation vaccines and therapeutic monoclonal antibodies to treat severe measles infections or complications like subacute sclerosing panencephalitis (SSPE) (Petrova et al., 2015). The interaction between the BCR and viral antigens triggers intracellular signaling pathways that result in B-cell proliferation and class-switch recombination to ensure high-affinity IgG production.
Antigen-mediated activation of B-cells leading to clonal expansion and secretion of neutralizing antibodies that inhibit viral attachment and membrane fusion (Janeway et al., 2001).
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