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Article

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

Virology - 1 Oct 2004

Zhang Xinyong, Kielian Margaret

Abstract excerpt

The enveloped alphavirus Semliki Forest virus (SFV) infects cells via a low pH-triggered membrane fusion reaction mediated by the E1 protein. E1's fusion activity is regulated by its heterodimeric interaction with a companion membrane protein E2. Mature E2 protein is generated by furin processing of the precursor p62. Processing destabilizes the heterodimer, allowing dissociation at acidic pH, E1 conformational...

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Identifiers

PMID: 15351216
DOI: 10.1016/j.virol.2004.06.037

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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.

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Mutations that promote furin-independent growth of Semliki Forest virus affect p62-E1 interactions and membrane fusion.PMID 15351216Read ↗

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

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

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

Processing of the p62 envelope precursor protein of Semliki Forest virus.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 Alphavirus E2 Membrane-Proximal Domain Promotes Envelope Protein Lateral Interactions and Virus Budding.Semantic proximity Read ↗

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

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