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The nucleocapsid proteins of varicella-zoster virus (VZV) form the icosahedral capsid shell, approximately 100-125 nm in diameter, enclosing the viral DNA genome. Composed primarily of major capsid protein (MCP), small capsid protein (SCP), and heterotriplex proteins Tri1 and Tri2, these proteins assemble into pentons, hexons, and heterotriplexes to maintain structural integrity during genome packaging, nuclear egress, and axonal transport for latency in neurons. A-, B-, and C-capsids represent assembly intermediates, with A-capsids being empty scaffolds. The capsid architecture is conserved among herpesviruses, with MCP featuring HK97-like folds, N-lassos, and conformational flexibility to withstand genome pressure. Alphaherpesvirus-specific features include SCP hairpin loops and flexible Tri1 N-anchors. The structure supports antiviral targeting, as seen with inhibitors disrupting MCP N-terminus assembly.
Impairs viral capsid assembly
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