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Conserved surface features on respiratory viruses refer to invariant structural motifs or epitopes found on the surface glycoproteins of viruses such as Influenza, SARS-CoV-2, and Respiratory Syncytial Virus (RSV). These features, often located in functional domains like the Hemagglutinin (HA) stalk or the S2 subunit of the Spike protein, are critical for viral entry and membrane fusion. Because these regions are essential for the viral life cycle, they are less prone to mutation compared to highly variable regions like the receptor-binding domain. Targeting these conserved features is a primary strategy for developing universal vaccines and broadly neutralizing antibodies (bnAbs) that can provide protection against multiple strains or emerging variants. Therapeutic intervention typically involves blocking the conformational changes required for fusion or preventing the virus from attaching to host cell receptors.
Neutralization of viral particles, inhibition of viral-host membrane fusion, blocking of receptor-binding domain (RBD) interactions, and induction of antibody-dependent cellular cytotoxicity (ADCC).
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