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The **Poliovirus type 3 capsid protein VP1-VP4 complex** forms the outer shell of poliovirus particles. The mature virion contains 60 copies each of four polypeptides—VP1, VP2, VP3 on the exterior surface and VP4 on the interior surface—arranged into an icosahedral structure that encases and protects the single-stranded positive-sense RNA genome[2][5]. These proteins assemble into pentamers which then form a complete procapsid during virus assembly. The N termini of these subunits contribute to internal surfaces while their C termini help form external features such as canyons around each vertex that interact with host cell receptors like PVR/CD155 to initiate infection[1][4]. This structural complex is essential for both protecting viral genetic material outside cells and mediating attachment/entry into susceptible human cells. It is considered a therapeutic target because disrupting its integrity or function can prevent infection by blocking entry or uncoating steps critical for viral replication[5].
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