ArticleThe EMBO journal2017
Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein.
Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Review
- Structures of vesicular stomatitis virus glycoprotein G alone and bound to a neutralizing antibody.PLoS pathogens · 2025Article
- Genomic and Structural Insights into Chandipura Virus: A Comparative in Silico Analysis of Indian and West African Strains and Potential Host Receptor Interactions.Current microbiology · 2025Article
- Viral fusion proteins of classes II and III recognize and reorganize complex biological membranes.Communications biology · 2025Article
- Structures of two lyssavirus glycoproteins trapped in pre- and post-fusion states and the implications on the spatial-temporal conformational transition along with pH-decrease.PLoS pathogens · 2025Article
- Capturing intermediates and membrane remodeling in class III viral fusion.Science advances · 2024Article
- Visualizing intermediate stages of viral membrane fusion by cryo-electron tomography.Trends in biochemical sciences · 2024Review
- Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch.Nature communications · 2024Article
- Viral Membrane Fusion: A Dance Between Proteins and Lipids.Annual review of virology · 2023Review
- Structure of trimeric pre-fusion rabies virus glycoprotein in complex with two protective antibodies.Cell host & microbe · 2022Article
- Analysis of the dark proteome of Chandipura virus reveals maximum propensity for intrinsic disorder in phosphoprotein.Scientific reports · 2021Article
- Mass Spectrometry-Based Structural Virology.Analytical chemistry · 2021Review
- The prefusion structure of herpes simplex virus glycoprotein B.Science advances · 2020Article
- Crystal structure of Mokola virus glycoprotein in its post-fusion conformation.PLoS pathogens · 2020Article
- Different functional states of fusion protein gB revealed on human cytomegalovirus by cryo electron tomography with Volta phase plate.PLoS pathogens · 2018Article
- Characterization of Antibody Interactions with the G Protein of Vesicular Stomatitis Virus Indiana Strain and Other Vesiculovirus G Proteins.Journal of virology · 2018Article
- Lentivector Producer Cell Lines with Stably Expressed Vesiculovirus Envelopes.Molecular therapy. Methods & clinical development · 2018Article
- Monomeric Intermediates Formed by Vesiculovirus Glycoprotein during Its Low-pH-induced Structural Transition.Journal of molecular biology · 2018Review
- Structural basis for the recognition of LDL-receptor family members by VSV glycoprotein.Nature communications · 2018Article
- Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein.The EMBO journal · 2017Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Vesiculoviruses enter cells by membrane fusion, driven by a large, low-pH-induced, conformational change in the fusion glycoprotein G that involves transition from a trimeric pre-fusion toward a trimeric post-fusion state via monomeric intermediates. Here, we present the structure of the G fusion protein at intermediate pH for two vesiculoviruses, vesicular stomatitis virus (VSV) and Chandipura virus (CHAV), which is responsible for deadly encephalopathies. First, a CHAV G crystal structure shows two intermediate conformations forming a flat dimer of heterodimers. On virions, electron microscopy (EM) and tomography reveal monomeric spikes similar to one of the crystal conformations. In solution, mass spectrometry shows dimers of G. Finally, mutations at a dimer interface, involving fusion domains associated in an antiparallel manner to form an intermolecular β-sheet, affect G fusion properties. The location of the compensatory mutations restoring fusion activity strongly suggests that this interface is functionally relevant. This work reveals the range of G structural changes and suggests that G monomers can re-associate, through antiparallel interactions between fusion domains, into dimers that play a role at some early stage of the fusion process.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.