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Enterovirus A71 (EV-A71) capsid conformational epitopes are complex three-dimensional structures on the viral surface formed by the assembly of structural proteins VP1, VP2, and VP3 [Scientific Reports, 2021; ResearchGate, 2016]. These epitopes serve as the primary targets for neutralizing antibodies and are the basis for the protective immunity elicited by inactivated EV-A71 vaccines [NIH, 2023]. Biologically, these regions are critical for viral attachment to host cell receptors, such as scavenger receptor class B2 (SCARB2) and P-selectin glycoprotein ligand-1 (PSGL-1), and they undergo significant structural rearrangements during the uncoating process to facilitate genome release [NIH, 2024; NIH, 2017]. EV-A71 is a major etiological agent of hand, foot, and mouth disease (HFMD), which can progress to severe neurological complications including brainstem encephalitis and acute flaccid paralysis [NIH, 2017; ResearchGate, 2024]. Therapeutic interventions targeting these epitopes include vaccines and experimental small-molecule capsid inhibitors like pleconaril and pocapavir, which stabilize the capsid to prevent infection [NIH, 2021; MDPI, 2022]. However, the high mutation rate of EV-A71 allows for the emergence of antigenic variants and escape mutants, posing a significant challenge for long-term vaccine efficacy and drug development [ASM, 2015; NIH, 2021].
Neutralization of viral infectivity by blocking receptor binding, inhibition of viral uncoating through capsid stabilization, and prevention of viral attachment to host cells [NIH, 2021; MDPI, 2022].
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