ArticleJournal of virology2009
E1 mutants identify a critical region in the trimer interface of the Semliki forest virus fusion protein.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 22 citations in OpenAlex.
- Visualization of conformational changes and membrane remodeling leading to genome delivery by viral class-II fusion machinery.Nature communications · 2022Article
- HAP2-Mediated Gamete Fusion: Lessons From the World of Unicellular Eukaryotes.Frontiers in cell and developmental biology · 2021Review
- AnmBio · 2017Article
- Intercellular Extensions Are Induced by the Alphavirus Structural Proteins and Mediate Virus Transmission.PLoS pathogens · 2016Article
- Fusion of Enveloped Viruses in Endosomes.Traffic (Copenhagen, Denmark) · 2016Review
- 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
- Rubella virus: first calcium-requiring viral fusion protein.PLoS pathogens · 2014Article
- Structural characterization of the glycoprotein GP2 core domain from the CAS virus, a novel arenavirus-like species.Journal of molecular biology · 2014Article
- Chikungunya fever: epidemiology, clinical syndrome, pathogenesis and therapy.Antiviral research · 2013Review
- 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
- Role of electrostatic repulsion in controlling pH-dependent conformational changes of viral fusion proteins.Structure (London, England : 1993) · 2013Review
- A tyrosine-to-histidine switch at position 18 of the Ross River virus E2 glycoprotein is a determinant of virus fitness in disparate hosts.Journal of virology · 2013Article
- Crystal structure of the Marburg virus GP2 core domain in its postfusion conformation.Biochemistry · 2012Article
- Identification of a specific region in the e1 fusion protein involved in zinc inhibition of semliki forest virus fusion.Journal of virology · 2012Article
- The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusion.Journal of virology · 2011Article
- Pseudorevertants of a Semliki forest virus fusion-blocking mutation reveal a critical interchain interaction in the core trimer.Journal of virology · 2010Article
- Alphavirus Entry and Membrane Fusion.Viruses · 2010Article
- Targeting lentiviral vector to specific cell types through surface displayed single chain antibody and fusogenic molecule.Virology journal · 2010Article
- Dealing with low pH: entry and exit of alphaviruses and flaviviruses.Trends in microbiology · 2009Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The alphavirus Semliki Forest virus (SFV) uses a membrane fusion reaction to infect host cells. Fusion of the virus and cell membranes is triggered by low pH in the endosome and is mediated by the viral membrane protein E1. During fusion, E1 inserts into the target membrane, trimerizes, and refolds into a hairpin conformation. Formation of the E1 homotrimer is critical to membrane fusion, but the mechanism of trimerization is not understood. The crystal structure of the postfusion E1 trimer shows that an aspartate residue, D188, is positioned in the central core trimer interface. D188 is conserved in all reported alphavirus E1 sequences. We tested the contribution of this amino acid to trimerization and fusion by replacing D188 with alanine (D188A) or lysine (D188K) in an SFV infectious clone. These mutations were predicted to disrupt specific interactions at this position and/or change their pH dependence. Our results indicated that the D188K mutation blocked SFV fusion and infection. At low pH, D188K E1 inserted into target membranes but was trapped as a target membrane-inserted monomer that did not efficiently form the stable core trimer. In contrast, the D188A mutant was infectious, although trimerization and fusion required a lower pH. While there are extensive contacts between E1 subunits in the homotrimer, the D188K mutant identifies an important "hot spot" for protein-protein interactions within the core trimer.
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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.