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The virus-host interface via vaccine-elicited antibodies represents the functional site where the humoral immune response intercepts viral particles to prevent infection [PubMed: 32405061]. This interface involves the binding of antibodies to viral glycoproteins, such as the SARS-CoV-2 spike protein, which blocks their interaction with host cell receptors like ACE2 [Nature: 10.1038/s41586-020-2852-1]. By occupying these critical binding sites, vaccine-elicited antibodies neutralize the virus and prevent the fusion of viral and cellular membranes [Science: 10.1126/science.abe3354]. This interaction is the primary mechanism by which vaccines provide protection against a wide range of viral pathogens, including influenza and respiratory syncytial virus [NIH: Vaccine Types]. Understanding the structural biology of this interface is essential for designing 'universal' vaccines that target conserved, non-mutating regions of the virus [Cell: 10.1016/j.cell.2021.04.011]. While not a single molecule, this interface is the focal point for evaluating vaccine efficacy and the impact of emerging viral variants.
Neutralization of viral entry by sterically blocking receptor binding or inhibiting membrane fusion.
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