Cryo-EM structure of the varicella-zoster virus A-capsid
| Autor: | Zhennan Zhao, Sheng Liu, Fu-Kun Zhang, Jianxun Qi, Xiaoming Yang, Min-Hua Luo, George F. Gao, Yi Shi, Congcong Liu, Wen-Bo Zeng, Junqing Sun, Peiyi Wang, Ruchao Peng, Hong-Jie Shen, Zhou Tong |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Models Molecular Herpesvirus 3 Human Subfamily Cryo-electron microscopy Protein Conformation viruses Science Protein domain General Physics and Astronomy medicine.disease_cause General Biochemistry Genetics and Molecular Biology Virus Article Cell Line 03 medical and health sciences 0302 clinical medicine Protein structure Capsid Protein Domains Cryoelectron microscopy Alphaherpesvirinae medicine Humans Herpes virus lcsh:Science Multidisciplinary biology integumentary system Varicella zoster virus virus diseases General Chemistry Virus structures biochemical phenomena metabolism and nutrition biology.organism_classification Virology 030104 developmental biology lcsh:Q Capsid Proteins 030217 neurology & neurosurgery |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | Varicella-zoster virus (VZV), a member of the Alphaherpesvirinae subfamily, causes severe diseases in humans of all ages. The viral capsids play critical roles in herpesvirus infection, making them potential antiviral targets. Here, we present the 3.7-Å-resolution structure of the VZV A-capsid and define the molecular determinants underpinning the assembly of this complicated viral machinery. Overall, the VZV capsid has a similar architecture to that of other known herpesviruses. The major capsid protein (MCP) assembles into pentons and hexons, forming extensive intra- and inter-capsomer interaction networks that are further secured by the small capsid protein (SCP) and the heterotriplex. The structure reveals a pocket beneath the floor of MCP that could potentially be targeted by antiviral inhibitors. In addition, we identified two alphaherpesvirus-specific structural features in SCP and Tri1 proteins. These observations highlight the divergence of different herpesviruses and provide an important basis for developing antiviral drugs. Varicella-zoster virus (VZV) is the causative agent of chickenpox and herpes zoster (shingles). Cryo-EM structure of VZV capsid provides insights into the capsid assembly and reveals a pocket that could potentially be targeted by antiviral drugs. |
| Databáze: | OpenAIRE |
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