Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery.

ABSTRACT: The herpesvirus capsid is a complex protein assembly that includes hundreds of copies of four major subunits and lesser numbers of several minor proteins, all of which are essential for infectivity. Cryo-electron microscopy is uniquely suited for studying interactions that govern the assembly and function of such large functional complexes. Here we report two high-quality capsid structures, from human herpes simplex virus type 1 (HSV-1) and the animal pseudorabies virus (PRV), imaged inside intact virions at ~7-Å resolution. From these, we developed a complete model of subunit and domain organization and identified extensive networks of subunit contacts that underpin capsid stability and form a pathway that may signal the completion of DNA packaging from the capsid interior to outer surfac

SUBMITTER: Huet A 

PROVIDER: S-EPMC4899274 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature