ArticleJournal of virology1991
Mutagenesis of the putative fusion domain of the Semliki Forest virus spike protein.
Article in Journal of virology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 117 citations in OpenAlex.
- Changes in the chikungunya virus E1 glycoprotein domain II and hinge influence E2 conformation, infectivity, and virus-receptor interactions.Journal of virology · 2024Article
- Article
- Two Conserved Phenylalanine Residues in the E1 Fusion Loop of Alphaviruses Are Essential for Viral Infectivity.Journal of virology · 2022Article
- Dynamics of natural product Lupenone as a potential fusion inhibitor against the spike complex of novel Semliki Forest Virus.PloS one · 2022Article
- Identification of Quinolinones as Antivirals against Venezuelan Equine Encephalitis Virus.Antimicrobial agents and chemotherapy · 2021Article
- Detection, isolation, and characterization of chikungunya viruses associated with the Pakistan outbreak of 2016-2017.Virologica Sinica · 2017Article
- Structure and interaction with lipid membrane models of Semliki Forest virus fusion peptide.Biochimica et biophysica acta · 2016Article
- The role of E3 in pH protection during alphavirus assembly and exit.Journal of virology · 2013Article
- Functional characterization of the alphavirus TF protein.Journal of virology · 2013Article
- A key interaction between the alphavirus envelope proteins responsible for initial dimer dissociation during fusion.Journal of virology · 2013Article
- Cell-based analysis of Chikungunya virus E1 protein in membrane fusion.Journal of biomedical science · 2012Article
- The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusion.Journal of virology · 2011Article
- An alternative pathway for alphavirus entry.Virology journal · 2011Review
- Antibody to the E3 glycoprotein protects mice against lethal venezuelan equine encephalitis virus infection.Journal of virology · 2010Article
- Pseudorevertants of a Semliki forest virus fusion-blocking mutation reveal a critical interchain interaction in the core trimer.Journal of virology · 2010Article
- La Crosse virus (LACV) Gc fusion peptide mutants have impaired growth and fusion phenotypes, but remain neurotoxic.Virology · 2010Article
- Alphavirus Entry and Membrane Fusion.Viruses · 2010Article
- E1 mutants identify a critical region in the trimer interface of the Semliki forest virus fusion protein.Journal of virology · 2009Article
- Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm.Retrovirology · 2008Review
- Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B.Journal of virology · 2007Article
7 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
Funding
Abstract
Semliki Forest virus (SFV), an alphavirus, infects cells via a low pH-triggered membrane fusion reaction that takes place within the cellular endocytic pathway. Fusion is mediated by the heterotrimeric virus spike protein, which undergoes conformational changes upon exposure to low pH. The SFV E1 spike subunit contains a hydrophobic domain of 23 amino acids that is highly conserved among alphaviruses. This region is also homologous to a domain of the rotavirus outer capsid protein VP4. Mutagenesis of an SFV spike protein cDNA was used to evaluate the role of the E1 domain in membrane fusion. Mutant spike proteins were expressed in COS cells and assayed for cell-cell fusion activity. Four mutant phenotypes were identified: (i) substitution of Gln for Lys-79 or Leu for Met-88 had no effect on spike protein fusion activity; (ii) substitution of Ala for Asp-75, Ala for Gly-83, or Ala for Gly-91 shifted the pH threshold of fusion to a more acidic range; (iii) mutation of Pro-86 to Asp, Gly-91 to Pro, or deletion of amino acids 83 to 92 resulted in retention of the E1 subunit within the endoplasmic reticulum; and (iv) substitution of Asp for Gly-91 completely blocked cell-cell fusion activity without affecting spike protein assembly or transport. These results argue that the conserved hydrophobic domain of SFV E1 is closely involved in membrane fusion and suggest that the homologous region in rotavirus VP4 may be involved in the entry pathway of this nonenveloped virus.
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