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TitleCryo-EM structure of a herpesvirus capsid at 3.1 Å.
Journal, issue, pagesScience, Vol. 360, Issue 6384, Year 2018
Publish dateApr 6, 2018
AuthorsShuai Yuan / Jialing Wang / Dongjie Zhu / Nan Wang / Qiang Gao / Wenyuan Chen / Hao Tang / Junzhi Wang / Xinzheng Zhang / Hongrong Liu / Zihe Rao / Xiangxi Wang /
PubMed AbstractStructurally and genetically, human herpesviruses are among the largest and most complex of viruses. Using cryo-electron microscopy (cryo-EM) with an optimized image reconstruction strategy, we ...Structurally and genetically, human herpesviruses are among the largest and most complex of viruses. Using cryo-electron microscopy (cryo-EM) with an optimized image reconstruction strategy, we report the herpes simplex virus type 2 (HSV-2) capsid structure at 3.1 angstroms, which is built up of about 3000 proteins organized into three types of hexons (central, peripentonal, and edge), pentons, and triplexes. Both hexons and pentons contain the major capsid protein, VP5; hexons also contain a small capsid protein, VP26; and triplexes comprise VP23 and VP19C. Acting as core organizers, VP5 proteins form extensive intermolecular networks, involving multiple disulfide bonds (about 1500 in total) and noncovalent interactions, with VP26 proteins and triplexes that underpin capsid stability and assembly. Conformational adaptations of these proteins induced by their microenvironments lead to 46 different conformers that assemble into a massive quasisymmetric shell, exemplifying the structural and functional complexity of HSV.
External linksScience / PubMed:29622627
MethodsEM (single particle)
Resolution3.1 Å
Structure data

6907

5zap

EMDB-6907, PDB-5zap:
Atomic structure of the herpes simplex virus type 2 B-capsid
Method: EM (single particle) / Resolution: 3.1 Å

Source
  • human herpesvirus 2
KeywordsVIRUS / herpesvirus / capsid / cryo-em / atomic structure

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