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The intact SARS-CoV-2 virion surface is the primary interface between the virus and the host, composed of a host-derived lipid bilayer embedded with structural proteins [V'kovski et al., 2021]. The Spike (S) glycoprotein is the most critical component, as it mediates binding to the host receptor Angiotensin-Converting Enzyme 2 (ACE2) and facilitates viral entry via membrane fusion [Hoffmann et al., 2020]. Other structural proteins on the surface include the Membrane (M) protein, which provides structural integrity, and the Envelope (E) protein, which is involved in viral assembly and budding [Schoeman & Fielding, 2019]. This surface is the main target for the host immune response, specifically for neutralizing antibodies that block the Spike protein's interaction with ACE2 [Kyriakidis et al., 2021]. Therapeutic interventions targeting the virion surface include monoclonal antibodies and vaccines designed to elicit a robust anti-Spike response [Hansen et al., 2020]. Additionally, the lipid envelope is susceptible to physical disruption by virucidal agents such as alcohols and detergents [Kampf et al., 2020]. Understanding the structural dynamics of the virion surface is essential for developing effective countermeasures against COVID-19 and monitoring the impact of emerging variants [V'kovski et al., 2021].
Neutralization of viral entry by binding to surface proteins (primarily Spike) to prevent ACE2 interaction or membrane fusion; physical disruption of the viral envelope [Hansen et al., 2020; Kampf et al., 2020].
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