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Article

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

Journal of virology - 1 May 2009

Qin Zhao-Ling, Zheng Yan, Kielian Margaret

Abstract excerpt

A wide variety of enveloped viruses infects cells by taking advantage of the low pH in the endocytic pathway to trigger virus-membrane fusion. For alphaviruses such as Semliki Forest virus (SFV), acidic pH initiates a series of conformational changes in the heterodimeric virus envelope proteins E1 and E2. Low pH dissociates the E2/E1 dimer, releasing the membrane fusion protein E1. E1 inserts into the target...

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Source

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Identifiers

PMID: 19244325
DOI: 10.1128/JVI.02646-08
PMCID: PMC2668505

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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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Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein.PMID 19244325Read ↗

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

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

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

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