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Article

Processing of the p62 envelope precursor protein of Semliki Forest virus.

The Journal of biological chemistry - 25 Mar 1991

Jain S K, DeCandido S, Kielian M

Abstract excerpt

The spike protein of Semliki Forest virus is composed of three subunits, E1, E2, and E3, which mediate the fusion of the virus membrane with that of the host cell. E2 and E3 are synthesized as a precursor, p62, which is cleaved post-translationally after an Arg-His-Arg-Arg sequence. In vitro mutagenesis of a cDNA clone of the spike proteins was used to specifically alter amino acids in this cleavage site....

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PMID: 2005112

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Processing of the p62 envelope precursor protein of Semliki Forest virus.PMID 2005112Read ↗

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

Spike protein oligomerization control of Semliki Forest virus fusion.Semantic proximity Read ↗

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

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 ↗

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

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

Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin.Semantic proximity Read ↗

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

African Swine Fever Virus Polyproteins pp220 and pp62 Assemble into the Core ShellSemantic proximity Read ↗

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