Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
Copyright policy )Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
AbstractAlphaviruses 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.
- Yunnan Animal Science and Veterinary Institute China (People's Republic of)
- Institute of Biophysics China (People's Republic of)
- State Key Laboratory of Veterinary Biotechnology China (People's Republic of)
- University of Science and Technology of China China (People's Republic of)
- Chinese Academy of Agricultural Sciences China (People's Republic of)
Models, Molecular, Life Cycle Stages, Membrane Glycoproteins, Protein Conformation, Science, Virus Assembly, Q, Cryoelectron Microscopy, Virion, Alphavirus, Virus Internalization, Crystallography, X-Ray, Article, Viral Envelope Proteins, Chlorocebus aethiops, Animals, Protein Interaction Domains and Motifs, Sindbis Virus, Vero Cells
Models, Molecular, Life Cycle Stages, Membrane Glycoproteins, Protein Conformation, Science, Virus Assembly, Q, Cryoelectron Microscopy, Virion, Alphavirus, Virus Internalization, Crystallography, X-Ray, Article, Viral Envelope Proteins, Chlorocebus aethiops, Animals, Protein Interaction Domains and Motifs, Sindbis Virus, Vero Cells
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).64 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 1% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!