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TitleNear-atomic cryo-electron microscopy structures of varicella-zoster virus capsids.
Journal, issue, pagesNat Microbiol, Vol. 5, Issue 12, Page 1542-1552, Year 2020
Publish dateSep 7, 2020
AuthorsWei Wang / Qingbing Zheng / Dequan Pan / Hai Yu / Wenkun Fu / Jian Liu / Maozhou He / Rui Zhu / Yuze Cai / Yang Huang / Zhenghui Zha / Zhenqin Chen / Xiangzhong Ye / Jinle Han / Yuqiong Que / Ting Wu / Jun Zhang / Shaowei Li / Hua Zhu / Z Hong Zhou / Tong Cheng / Ningshao Xia /
PubMed AbstractVaricella-zoster virus (VZV) is a medically important human herpesvirus that causes chickenpox and shingles, but its cell-associated nature has hindered structure studies. Here we report the cryo- ...Varicella-zoster virus (VZV) is a medically important human herpesvirus that causes chickenpox and shingles, but its cell-associated nature has hindered structure studies. Here we report the cryo-electron microscopy structures of purified VZV A-capsid and C-capsid, as well as of the DNA-containing capsid inside the virion. Atomic models derived from these structures show that, despite enclosing a genome that is substantially smaller than those of other human herpesviruses, VZV has a similarly sized capsid, consisting of 955 major capsid protein (MCP), 900 small capsid protein (SCP), 640 triplex dimer (Tri2) and 320 triplex monomer (Tri1) subunits. The VZV capsid has high thermal stability, although with relatively fewer intra- and inter-capsid protein interactions and less stably associated tegument proteins compared with other human herpesviruses. Analysis with antibodies targeting the N and C termini of the VZV SCP indicates that the hexon-capping SCP-the largest among human herpesviruses-uses its N-terminal half to bridge hexon MCP subunits and possesses a C-terminal flexible half emanating from the inner rim of the upper hexon channel into the tegument layer. Correlation of these structural features and functional observations provide insights into VZV assembly and pathogenesis and should help efforts to engineer gene delivery and anticancer vectors based on the currently available VZV vaccine.
External linksNat Microbiol / PubMed:32895526 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 6.3 Å
Structure data

0880

6lgl

EMDB-0880, PDB-6lgl:
The atomic structure of varicella-zoster virus A-capsid
Method: EM (single particle) / Resolution: 4.4 Å

0881

6lgn

EMDB-0881, PDB-6lgn:
The atomic structure of varicella zoster virus C-capsid
Method: EM (single particle) / Resolution: 5.3 Å

EMDB-30248:
CryoEM structure of VZV A-capsid, 3-fold sub-particle reconstruction
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-30250:
CryoEM structure of VZV C-capsid, 3-fold sub-particle reconstruction
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-30251:
CryoEM structure of VZV capsid derived from virion
Method: EM (single particle) / Resolution: 6.3 Å

Source
  • human herpesvirus 3 (Varicella-zoster virus)
KeywordsVIRUS / Herpesvirus / varicella-zoster virus / capsid / Varicella zoster virus / C-capsid

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