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The Poliovirus type 2 capsid is a non-enveloped, icosahedral protein shell comprising 60 copies each of the viral proteins VP1, VP2, VP3, and VP4. It surrounds and protects the viral RNA genome and mediates attachment to the cellular poliovirus receptor (CD155), controlling cell entry and infection. The surface of the capsid contains distinct antigenic sites that are targets for neutralizing antibodies, making the capsid the primary target for protective immunity induced by polio vaccines. During viral entry, receptor binding induces conformational changes in the capsid that facilitate RNA release into the host cell cytoplasm. The capsid's critical biological and immunological properties make it a central focus for vaccine design, serological monitoring, and fundamental virology studies.
Neutralizing antibodies bind to surface-exposed loops (antigenic/neutralization sites) on the capsid, preventing attachment to the host cell receptor or blocking conformational changes required for viral entry. Experimental capsid inhibitors would act by stabilizing the capsid or interfering with the uncoating process, though this is not an established therapy for poliovirus.
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