ArticleJournal of virology2004
A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 63 citations in OpenAlex.
- Structural and antigenic characterization of Babesia Bovis HAP2 domains.Scientific reports · 2025Article
- Changes in the chikungunya virus E1 glycoprotein domain II and hinge influence E2 conformation, infectivity, and virus-receptor interactions.Journal of virology · 2024Article
- The La Crosse virus class II fusion glycoproteinJournal of virology · 2023Article
- Visualization of conformational changes and membrane remodeling leading to genome delivery by viral class-II fusion machinery.Nature communications · 2022Article
- Structurally Conserved Domains between Flavivirus and Alphavirus Fusion Glycoproteins Contribute to Replication and Infectious-Virion Production.Journal of virology · 2022Article
- Membranotropic peptides mediating viral entry.Peptide science (Hoboken, N.J.) · 2018Review
- Identification of determinants that mediate binding between Tembusu virus and the cellular receptor heat shock protein A9.Journal of veterinary science · 2018Article
- AnmBio · 2017Article
- Antiviral activities of niclosamide and nitazoxanide against chikungunya virus entry and transmission.Antiviral research · 2016Article
- Single-Site Glycoprotein Mutants Inhibit a Late Event in Sindbis Virus Assembly.Journal of virology · 2016Article
- Calcium-Dependent Rubella Virus Fusion Occurs in Early Endosomes.Journal of virology · 2016Article
- An alphavirus temperature-sensitive capsid mutant reveals stages of nucleocapsid assembly.Virology · 2015Article
- 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
- gH625: a milestone in understanding the many roles of membranotropic peptides.Biochimica et biophysica acta · 2015Review
- Rubella virus: first calcium-requiring viral fusion protein.PLoS pathogens · 2014Article
- A histidine residue of the influenza virus hemagglutinin controls the pH dependence of the conformational change mediating membrane fusion.Journal of virology · 2014Article
- Imaging the alphavirus exit pathway.Journal of virology · 2014Article
- Imaging of the alphavirus capsid protein during virus replication.Journal of virology · 2013Article
- Characterizing a histidine switch controlling pH-dependent conformational changes of the influenza virus hemagglutinin.Biophysical journal · 2013Article
- Role of electrostatic repulsion in controlling pH-dependent conformational changes of viral fusion proteins.Structure (London, England : 1993) · 2013Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The enveloped alphavirus Semliki Forest virus (SFV) infects cells via a low pH-triggered membrane fusion reaction mediated by the E1 protein. E1 is a class II fusion protein that contains the hydrophobic fusion peptide loop and converts to a stable homotrimer during the fusion reaction. Intriguingly, the fusion loop is closely associated with a loop connecting the i and j beta-strands. This ij loop plays a role in the cholesterol dependence of membrane fusion and is specifically susceptible to proteolysis in the protease-resistant E1 homotrimer. The SFV ij loop contains a histidine residue at position 230. Sequence comparisons revealed that an analogous histidine is completely conserved in all alphavirus and flavivirus fusion proteins. An E1 H230A mutant was constructed using the SFV infectious clone. Although cells infected with H230A RNA produced virus particles, these virions were completely noninfectious and were blocked in both cell-cell fusion and lipid mixing assays. The H230A virions efficiently bound to cell surface receptors and responded to low pH by undergoing acid-dependent conformational changes including dissociation of the E1/E2 dimer, exposure of the fusion loop, association with target liposomes, exposure of acid-conformation-specific epitopes, and formation of the stable E1 homotrimer. Studies with a soluble fragment of E1 showed that the mutant protein was defective in lipid-dependent conformational changes. Our results indicate that the E1 ij loop and the conserved H230 residue play a critical role in alphavirus-membrane fusion and suggest the presence of a previously undescribed late intermediate in the fusion reaction.
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