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Conserved surface epitopes of influenza virus proteins are highly stable antigenic regions located on the viral envelope proteins, primarily the hemagglutinin (HA) stalk, the matrix protein 2 ectodomain (M2e), and specific sites on neuraminidase (NA) (NIH, 2014; MDPI, 2020). Unlike the immunodominant globular head of HA, which undergoes rapid antigenic drift, these conserved regions remain relatively unchanged across diverse influenza A and B strains (NIH, 2014; NIH, 2019). The biological function of these targets is critical for viral fitness; for instance, the HA stalk mediates the pH-dependent membrane fusion required for viral entry, while M2e is part of an ion channel essential for viral uncoating (Frontiers, 2021; NIH, 2019). Therapeutic strategies targeting these epitopes include broadly neutralizing antibodies (bnAbs) and universal vaccine candidates designed to elicit heterosubtypic immunity (NIH, 2009; NIH, 2019). Drugs such as MEDI8852 and VIR-2482 bind to these conserved sites to neutralize the virus by blocking entry or engaging host immune effector functions like antibody-dependent cellular cytotoxicity (ADCC) (NIH, 2014; NIH, 2019).
Neutralization of viral entry by blocking hemagglutinin-mediated membrane fusion or receptor binding, inhibition of viral release via neuraminidase targeting, and induction of Fc-mediated effector functions such as antibody-dependent cellular cytotoxicity (ADCC).
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