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The Human B-cell receptor (BCR) recognizing influenza hemagglutinin (HA) and neuraminidase (NA) epitopes is a membrane-bound immunoglobulin complex essential for the adaptive immune response against influenza viruses (Janeway et al., 2001). These receptors are expressed on the surface of B cells and are responsible for the initial recognition of viral surface glycoproteins. HA-specific BCRs typically target the globular head or the conserved stem region of hemagglutinin to prevent viral attachment and fusion, while NA-specific BCRs target the neuraminidase enzyme to inhibit the release of progeny virions from infected cells (Krammer, 2019). Upon binding to these viral antigens, the BCR initiates signaling pathways—mediated by the CD79A/B heterodimer—that drive the expansion of influenza-specific B cell clones and the production of high-affinity neutralizing antibodies (Victora & Nussenzweig, 2012). This target is the primary focus of seasonal and universal influenza vaccine strategies, which aim to elicit broad and potent BCR responses to provide long-lasting protection against diverse viral strains (Ellebedy et al., 2016). Understanding the repertoire and specificity of these receptors is crucial for developing next-generation immunotherapies and vaccines that can overcome viral evolution (Kim et al., 2009).
Antigen-induced cross-linking of the B-cell receptor (BCR) triggers intracellular signaling via the Ig-alpha/Ig-beta (CD79A/CD79B) heterodimer, leading to B-cell activation, proliferation, and differentiation into antibody-secreting plasma cells and memory B cells [1, 2].
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