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Article

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

Journal of virology - 1 Oct 1990

Kielian M, Jungerwirth S, Sayad K U, DeCandido S

Abstract excerpt

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...

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Source

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Identifiers

PMID: 2118964
DOI: 10.1128/JVI.64.10.4614-4624.1990
PMCID: PMC247945

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Biosynthesis, maturation, and acid activation of the Semliki Forest virus fusion protein.PMID 2118964Read ↗

Processing of the p62 envelope precursor protein of 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 ↗

Mechanisms of mutations inhibiting fusion and infection by 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 ↗

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

Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein.Semantic proximity Read ↗

The conserved glycine residues in the transmembrane domain of the Semliki Forest virus fusion protein are not required for assembly and fusion.Semantic proximity Read ↗

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

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

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

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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 ↗

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