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Enterovirus A71 viral proteins are encoded by the single-stranded, positive-sense RNA virus Enterovirus A71, a member of the Picornaviridae family and the primary causative agent of large outbreaks of hand, foot, and mouth disease (HFMD), especially in young children[1][2]. Its genome is translated into a single polyprotein (~2,100 amino acids), which is proteolytically cleaved into structural (VP1, VP2, VP3, VP4) and non-structural (2A, 2B, 2C, 3A, 3B/VPg, 3C, 3D) proteins[1][2][3]. The structural proteins form the icosahedral capsid, critical for cellular attachment via host receptors (notably PSGL-1 and SCARB2) and protection of the viral genome[1][2]. The non-structural proteins mediate polyprotein processing, replication complex formation, host immune modulation, and viral RNA replication[2]. Some EV-A71 proteins, especially the capsid protein VP1, are direct targets for therapeutic development (e.g., small-molecule capsid inhibitors) and vaccine formulations. EV-A71 protein expression correlates with viral load and disease severity, and some proteins are used as diagnostic biomarkers[2][4]. While "Enterovirus 71 viral proteins" refers collectively to a group of related proteins rather than a single molecular target, several individual proteins are well-validated antiviral targets, particularly VP1 (capsid), 3C protease, and 3D polymerase[1][2][4].\n\nClarification:\n- The entry "Enterovirus 71 viral proteins" is not a singular, well-defined drug target, but rather a set of viral protein products from the EV-A71 genome. Each protein (e.g., VP1, 3C protease, 3D polymerase) has its canonical form and may be a drug target individually[1][2].\n- For structured biomedical data, it is recommended to reference specific proteins (e.g., "Enterovirus A71 capsid protein VP1" or "Enterovirus A71 3C protease") for accuracy and consistency.
Inhibition of viral entry, Inhibition of viral protease activity, Inhibition of viral RNA polymerase
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