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Respiratory viral surface proteins are specialized glycoproteins and structures located on the exterior of viral particles, such as the Spike protein of SARS-CoV-2, Hemagglutinin and Neuraminidase of Influenza, and the Fusion (F) protein of Respiratory Syncytial Virus (RSV) (Cui et al., 2019; Skehel & Wiley, 2000). These proteins are essential for the viral life cycle, serving as the primary tools for recognizing and adhering to specific receptors on host respiratory epithelial cells (Battles & McLellan, 2019). Beyond attachment, many of these proteins undergo dramatic structural rearrangements to catalyze the fusion of the viral envelope with the host cell membrane, enabling the delivery of the viral genome into the cell (Harrison, 2008). Because they are the most accessible parts of the virus to the host immune system, they are the principal targets for neutralizing antibodies induced by vaccines or administered as therapeutic monoclonal antibodies (Graham, 2020). Pharmacological intervention typically involves small molecules or antibodies that sterically hinder receptor binding, inhibit fusion-inducing conformational changes, or block enzymatic activities necessary for viral release and spread.
Drugs targeting these proteins primarily function by blocking viral attachment to host receptors, inhibiting the fusion of viral and cellular membranes, or preventing the release of new viral progeny from the host cell surface.
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