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Poliovirus capsid surface antigens refer to the protein components exposed on the surface of the poliovirus particle, comprised mostly of the structural proteins VP1, VP2, and VP3, which form the outer shell of the nonenveloped virus. These proteins are responsible for critical interactions with the host cell receptor (CD155/PVR) for viral entry[1][5], define viral serotypes, and confer immunogenicity, making them the principal targets of neutralizing antibodies. The surface topography is characterized by the presence of mesas, canyons, and propeller-like features[3][4][7], with antigenic sites situated on specific exposed loops and domains of these capsid proteins[2][3]. Changes in these surface antigens—through mutation or drift—define poliovirus serotypes and influence immune evasion. Inactivated and live-attenuated vaccines act by eliciting antibodies that bind these antigens and prevent infection. Certain antivirals may also interact with conserved structural pockets beneath these antigenic surfaces to block conformational changes necessary for cell entry[5]. Safety concerns for therapeutics targeting these antigens include the risk of serotype-specific immune escape and adverse vaccine reactions.
Vaccine-induced antibody binding and neutralization\nDrug-induced blockade of capsid structural changes (for capsid-binding molecules)\nPrevention of receptor-mediated viral entry (by stabilizing the capsid antigenic site)
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