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Article

Spike protein oligomerization control of Semliki Forest virus fusion.

Journal of virology - 1 Oct 1990

Lobigs M, Wahlberg J M, Garoff H

Abstract excerpt

We have recently shown, using cleavage-deficient mutants of the p62-E1 membrane protein complex of Semliki Forest virus that p62 cleavage to E2 is necessary for the activation of the fusion function of the complex at pH 5.8 (a pH optimal for virus fusion) (M. Lobigs and H. Garoff, J. Virol. 64:1233-1240, 1990). In this study, we show that the mutant precursor complexes can be induced to activate membrane fusion...

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Identifiers

PMID: 2398543
DOI: 10.1128/JVI.64.10.5214-5218.1990
PMCID: PMC248021

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Spike protein oligomerization control of Semliki Forest virus fusion.PMID 2398543Read ↗

Processing of the p62 envelope precursor protein of Semliki Forest virus.Semantic proximity Read ↗

Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62.Semantic proximity Read ↗

The nucleocapsid-binding spike subunit E2 of Semliki Forest virus requires complex formation with the E1 subunit for activity.Semantic proximity Read ↗

Function of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1.Semantic proximity Read ↗

An interaction site of the envelope proteins of Semliki Forest virus that is preserved after proteolytic activation.Semantic proximity Read ↗

Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.Semantic proximity Read ↗

Differential roles of two conserved glycine residues in the fusion peptide of Semliki Forest virus.Semantic proximity Read ↗

Mutations that promote furin-independent growth of Semliki Forest virus affect p62-E1 interactions and membrane fusion.Semantic proximity Read ↗

Biosynthesis, maturation, and acid activation of the Semliki Forest virus fusion protein.Semantic proximity Read ↗

PE2 cleavage mutants of Sindbis virus: correlation between viral infectivity and pH-dependent membrane fusion activation of the spike heterodimer.Semantic proximity Read ↗

The dynamic envelope of a fusion class II virus. E3 domain of glycoprotein E2 precursor in Semliki Forest virus provides a unique contact with the fusion protein E1.Semantic proximity Read ↗

fus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunit.Semantic proximity Read ↗

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