ArticleThe EMBO journal2002
Acid-induced movements in the glycoprotein shell of an alphavirus turn the spikes into membrane fusion mode.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 37 citations in OpenAlex.
- High adenoviral vector concentration can cause irreversible aggregation during CsCl gradient ultracentrifugation.Frontiers in microbiology · 2026Article
- Visualization of conformational changes and membrane remodeling leading to genome delivery by viral class-II fusion machinery.Nature communications · 2022Article
- The Structural Biology of Eastern Equine Encephalitis Virus, an Emerging Viral Threat.Pathogens (Basel, Switzerland) · 2021Review
- A unified route for flavivirus structures uncovers essential pocket factors conserved across pathogenic viruses.Nature communications · 2021Article
- Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure.Nature communications · 2018Article
- Cryo-EM Structures of Eastern Equine Encephalitis Virus Reveal Mechanisms of Virus Disassembly and Antibody Neutralization.Cell reports · 2018Article
- Residue-level resolution of alphavirus envelope protein interactions in pH-dependent fusion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural differences observed in arboviruses of the alphavirus and flavivirus genera.Advances in virology · 2014Review
- Characterization of an early-stage fusion intermediate of Sindbis virus using cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A single amino acid substitution in the core protein of West Nile virus increases resistance to acidotropic compounds.PloS one · 2013Article
- Structural evidence of glycoprotein assembly in cellular membrane compartments prior to Alphavirus budding.Journal of virology · 2010Article
- Structure of a Venezuelan equine encephalitis virus assembly intermediate isolated from infected cells.Virology · 2010Article
- The dynamic envelope of a fusion class II virus. E3 domain of glycoprotein E2 precursor in Semliki Forest virus provides a unique contact with the fusion protein E1.The Journal of biological chemistry · 2008Article
- Sindbis virus conformational changes induced by a neutralizing anti-E1 monoclonal antibody.Journal of virology · 2008Article
- Reversible acid-induced inactivation of the membrane fusion protein of Semliki Forest virus.Journal of virology · 2005Article
- Molecular dynamics simulations of the E1/E2 transmembrane domain of the Semliki Forest virus.Biophysical journal · 2003Article
- Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion.Journal of virology · 2003Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the icosahedral (T = 4) Semliki Forest virus, the envelope protomers, i.e. E1-E2 heterodimers, make one-to-one interactions with capsid proteins below the viral lipid bilayer, transverse the membrane and form an external glycoprotein shell with projections. The shell is organized by protomer domains interacting as hexamers and pentamers around shell openings at icosahedral 2- and 5-fold axes, respectively, and the projections by other domains associating as trimers at 3- and quasi 3-fold axes. We show here, using cryo- electron microscopy, that low pH, as occurs in the endosomes during virus uptake, results in the relaxation of protomer interactions around the 2- and the 5-fold axes in the shell, and movement of protomers towards 3- and quasi 3-fold axes in a way that reciprocally relocates their putative E1 and E2 domains. This seemed to be facilitated by a trimerization of transmembrane segments at the same axes. The alterations observed help to explain several key features of the spike-mediated membrane fusion reaction, including shell dissolution, heterodimer dissociation, fusion peptide exposure and E1 homotrimerization.
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