ArticleJournal of virology2011
The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusion.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Structural and Functional Hallmarks of Sindbis Virus Proteins: From Virion Architecture to Pathogenesis.International journal of molecular sciences · 2025Review
- Hantavirus: an overview and advancements in therapeutic approaches for infection.Frontiers in microbiology · 2023Review
- Acidic pH-Induced Conformational Changes in Chikungunya Virus Fusion Protein E1: a Spring-Twisted Region in the Domain I-III Linker Acts as a Hinge Point for Swiveling Motion of Domains.Journal of virology · 2020Article
- A molecular understanding of alphavirus entry.PLoS pathogens · 2020Review
- Monomeric Intermediates Formed by Vesiculovirus Glycoprotein during Its Low-pH-induced Structural Transition.Journal of molecular biology · 2018Review
- Inhibition of the Hantavirus Fusion Process by Predicted Domain III and Stem Peptides from Glycoprotein Gc.PLoS neglected tropical diseases · 2016Article
- 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
- Hantavirus Gn and Gc envelope glycoproteins: key structural units for virus cell entry and virus assembly.Viruses · 2014Review
- Structural differences observed in arboviruses of the alphavirus and flavivirus genera.Advances in virology · 2014Review
- Cross-inhibition of chikungunya virus fusion and infection by alphavirus E1 domain III proteins.Journal of virology · 2013Article
- Intermediate conformations during viral fusion glycoprotein structural transition.Current opinion in virology · 2013Review
- Identification of a specific region in the e1 fusion protein involved in zinc inhibition of semliki forest virus fusion.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Alphaviruses such as Semliki Forest virus (SFV) are enveloped viruses that infect cells through a low-pH-triggered membrane fusion reaction mediated by the transmembrane fusion protein E1. E1 drives fusion by insertion of its hydrophobic fusion loop into the cell membrane and refolding to a stable trimeric hairpin. In this postfusion conformation, the immunoglobulin-like domain III (DIII) and the stem region pack against the central core of the trimer. Membrane fusion and infection can be specifically inhibited by exogenous DIII, which binds to an intermediate in the E1 refolding pathway. Here we characterized the properties of the E1 target for interaction with exogenous DIII. The earliest target for DIII binding was an extended membrane-inserted E1 trimer, which was not detectable by assays for the stable postfusion hairpin. DIII binding provided a tool to detect this extended trimer and to define a series of SFV fusion-block mutants. DIII binding studies showed that the mutants were blocked in distinct steps in fusion protein refolding. Our results suggested that formation of the initial extended trimer was reversible and that it was stabilized by the progressive fold-back of the DIII and stem regions.
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Registered trials
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.