ArticleJournal of virology1990
Biosynthesis, maturation, and acid activation of the Semliki Forest virus fusion protein.
Article in Journal of virology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 87 citations in OpenAlex.
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- Quantitative Proteomics of Uukuniemi Virus-host Cell Interactions Reveals GBF1 as Proviral Host Factor for Phleboviruses.Molecular & cellular proteomics : MCP · 2019Article
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- Intercellular Extensions Are Induced by the Alphavirus Structural Proteins and Mediate Virus Transmission.PLoS pathogens · 2016Article
- Calcium-Dependent Rubella Virus Fusion Occurs in Early Endosomes.Journal of virology · 2016Article
- Role of TSPAN9 in Alphavirus Entry and Early Endosomes.Journal of virology · 2016Article
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- An alphavirus temperature-sensitive capsid mutant reveals stages of nucleocapsid assembly.Virology · 2015Article
- Rubella virus: first calcium-requiring viral fusion protein.PLoS pathogens · 2014Article
- The role of E3 in pH protection during alphavirus assembly and exit.Journal of virology · 2013Article
- A key interaction between the alphavirus envelope proteins responsible for initial dimer dissociation during fusion.Journal of virology · 2013Article
- Genome-wide RNAi screen identifies novel host proteins required for alphavirus entry.PLoS pathogens · 2013Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Semliki Forest virus spike protein has a potent membrane fusion activity which is activated in vivo by the low pH of endocytic vacuoles. The spike protein is composed of two transmembrane subunits, E1 and E2, plus E3, a peripheral polypeptide. Acid-induced conformational changes in the E1 or E2 subunits were analyzed by using monoclonal antibodies specific for the acid-treated spike protein. E1 and E2 reacted with the antibodies after treatment of wild-type or mutant virus at the pH of fusion. The E1 conformational change resembled fusion in its requirement for both low pH and cholesterol. Pulse-chase analysis and intracellular pH treatment were then used to determine the ability of the newly synthesized spike to undergo acid-induced conformational changes. p62, the precursor to E2 and E3, was shown to undergo a pH-dependent conformational change similar to that of E2 and was sensitive to acid very soon after biosynthesis. In contrast, a posttranslational maturation event was required for the conversion of E1 to the pH-sensitive form. E1 maturation occurred fairly late in the exocytic pathway, after the virus spike had passed the medial Golgi but before incorporation of the spike into a new virus particle.
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Registered trials
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