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Article

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

Journal of virology - 1 May 1998

Glomb-Reinmund S, Kielian M

Abstract excerpt

Semliki Forest virus (SFV), an enveloped alphavirus, is a well-characterized paradigm for viruses that infect cells via endocytic uptake and low-pH-triggered fusion. The SFV spike protein is composed of a dimer of E1 and E2 transmembrane subunits, which dissociate upon exposure to low pH, liberating E2 and the fusogenic E1 subunit to undergo independent conformational changes. SFV fusion and infection are blocked...

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Identifiers

PMID: 9557718
DOI: 10.1128/JVI.72.5.4281-4287.1998
PMCID: PMC109658

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fus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunit.PMID 9557718Read ↗

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

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

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

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

An Alphavirus E2 Membrane-Proximal Domain Promotes Envelope Protein Lateral Interactions and Virus Budding.Semantic proximity Read ↗

A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion.Semantic proximity Read ↗

The domain I-domain III linker plays an important role in the fusogenic conformational change of the alphavirus membrane fusion protein.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 ↗

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