Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
| Autor: | S. Wang, J. L. Wang, Yunbin He, Junying Ma, Z. Sun, L. Wei, Xinzheng Zhang, Z. Liu, Dongjie Zhu, M. Wang, Lupeng Kong, L. Chen |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Sindbis virus Protein Conformation Cryo-electron microscopy viruses Science General Physics and Astronomy Alphavirus macromolecular substances Crystallography X-Ray Article General Biochemistry Genetics and Molecular Biology Virus 03 medical and health sciences 0302 clinical medicine Protein structure Viral Envelope Proteins Viral life cycle Chlorocebus aethiops Animals Protein Interaction Domains and Motifs lcsh:Science Vero Cells Life Cycle Stages Membrane Glycoproteins Multidisciplinary biology Chemistry Virus Assembly Cryoelectron Microscopy Virion RNA General Chemistry Virus Internalization Viral membrane biology.organism_classification Cell biology 030104 developmental biology lcsh:Q Sindbis Virus 030217 neurology & neurosurgery |
| Zdroj: | Nature Communications, Vol 9, Iss 1, Pp 1-8 (2018) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | Alphaviruses are enveloped RNA viruses that contain several human pathogens. Due to intrinsic heterogeneity of alphavirus particles, a high resolution structure of the virion is currently lacking. Here we provide a 3.5 Å cryo-EM structure of Sindbis virus, using block based reconstruction method that overcomes the heterogeneity problem. Our structural analysis identifies a number of conserved residues that play pivotal roles in the virus life cycle. We identify a hydrophobic pocket in the subdomain D of E2 protein that is stabilized by an unknown pocket factor near the viral membrane. Residues in the pocket are conserved in different alphaviruses. The pocket strengthens the interactions of the E1/E2 heterodimer and may facilitate virus assembly. Our study provides structural insights into alphaviruses that may inform the design of drugs and vaccines. Alphaviruses are enveloped RNA viruses that contain several human pathogens. Here, the authors use block-based reconstruction method and provide a 3.5 Å cryo-EM structure of sindbis virus that identifies a conserved hydrophobic pocket near the viral membrane that is stabilized by an unknown pocket factor. |
| Databáze: | OpenAIRE |
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