6LGL
The atomic structure of varicella-zoster virus A-capsid
This is a non-PDB format compatible entry.
Summary for 6LGL
| Entry DOI | 10.2210/pdb6lgl/pdb |
| EMDB information | 0880 |
| Descriptor | Major capsid protein, Small capsomere-interacting protein, Triplex capsid protein 1, ... (4 entities in total) |
| Functional Keywords | herpesvirus, varicella-zoster virus, capsid, virus |
| Biological source | Human herpesvirus 3 (HHV-3,Human alphaherpesvirus 3) More |
| Total number of polymer chains | 46 |
| Total formula weight | 3463287.57 |
| Authors | |
| Primary citation | Wang, W.,Zheng, Q.,Pan, D.,Yu, H.,Fu, W.,Liu, J.,He, M.,Zhu, R.,Cai, Y.,Huang, Y.,Zha, Z.,Chen, Z.,Ye, X.,Han, J.,Que, Y.,Wu, T.,Zhang, J.,Li, S.,Zhu, H.,Zhou, Z.H.,Cheng, T.,Xia, N. Near-atomic cryo-electron microscopy structures of varicella-zoster virus capsids. Nat Microbiol, 5:1542-1552, 2020 Cited by PubMed Abstract: 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. PubMed: 32895526DOI: 10.1038/s41564-020-0785-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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