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TitleExtensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery.
Journal, issue, pagesNat Struct Mol Biol, Vol. 23, Issue 6, Page 531-539, Year 2016
Publish dateApr 25, 2016
AuthorsAlexis Huet / Alexander M Makhov / Jamie B Huffman / Matthijn Vos / Fred L Homa / James F Conway /
PubMed AbstractThe 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. ...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 surface, thereby initiating nuclear egress. Differences in the folding and orientation of subunit domains between herpesvirus capsids suggest that common elements have been modified for specific functions.
External linksNat Struct Mol Biol / PubMed:27111889 / PubMed Central
MethodsEM (single particle)
Resolution6.8 - 7.2 Å
Structure data

EMDB-6386:
The capsid of Human Herpes Simplex Virus Type 1 imaged inside intact virions
Method: EM (single particle) / Resolution: 6.8 Å

EMDB-6387:
A new view of essential vertex proteins on herpesvirus capsids observed inside intact virions
Method: EM (single particle) / Resolution: 7.2 Å

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