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The Enterovirus D68 (EV-D68) capsid is a nonenveloped, icosahedral protein shell that encases the viral positive-sense single-stranded RNA genome. The capsid is composed of 60 copies each of four structural proteins: VP1, VP2, VP3, and VP4. These proteins assemble to form a particle approximately 300 Å in diameter. VP1, VP2, and VP3 are exposed on the outer surface of the capsid, while VP4 lines the interior surface. The capsid plays a critical role in receptor binding (e.g., to sialic acids, ICAM-5, sulfated glycosaminoglycans and MFSD6), cell entry, and uncoating, making it a key target for antiviral development. The most variable region among strains is found in the external loops of the VP1 protein, which determines serotype specificity and antigenicity.
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