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The surface proteins VP1, VP2, and VP3 of Enterovirus 71, Coxsackievirus A16, Coxsackievirus A10, and Coxsackievirus A6 form the outer shell of the viral capsid, which protects the viral RNA and mediates attachment and entry into host cells. These proteins assemble into icosahedral particles and display variable surface loops that define antigenic properties and receptor interactions. VP1, in particular, contains key neutralizing epitopes and forms the so-called “canyon” used for receptor engagement. Structural differences, especially in surface loops, help determine host range and immune escape; thus, they are the primary targets for vaccine and therapeutic antibody development. Capsid-binding small molecules also target conserved pockets in these proteins to block viral uncoating and entry. The antigenic and structural diversity between these viruses complicates broad-spectrum drug and vaccine development[2][3][4][6].
Inhibition of viral uncoating (capsid binders stabilize capsid)[2]; Virus neutralization (by antibody binding to critical epitopes)[4]
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