Second-site revertants of a Semliki Forest Virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein

Chantal Chanel-Vos, Margaret Kielian

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

The alphavirus Semliki Forest virus (SFV) infects cells through low-pH-induced membrane fusion mediated by the E1 protein, a class II virus membrane fusion protein. During fusion, E1 inserts into target membranes via its hydrophobic fusion loop and refolds to form a stable E1 homotrimer. Mutation of a highly conserved histidine (the H230A mutation) within a loop adjacent to the fusion loop was previously shown to block SFV fusion and infection, although the mutant E1 protein still inserts into target membranes and forms a homotrimer. Here we report on second-site mutations in E1 that rescue the H230A mutant. These mutations were located in a cluster within the hinge region, at the membrane-interacting tip, and within the groove where the E1 stem is believed to pack. Together the revertants reveal specific and interconnected aspects of the fusion protein refolding reaction.

Original languageEnglish (US)
Pages (from-to)6115-6122
Number of pages8
JournalJournal of Virology
Volume80
Issue number12
DOIs
StatePublished - Jun 2006

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Membrane Fusion Proteins
Semliki Forest virus
Semliki forest virus
mutation
Mutation
Membranes
proteins
Viral Fusion Proteins
Protein Refolding
Alphavirus
Virus Internalization
mutants
Membrane Fusion
Virus Diseases
Mutant Proteins
histidine
Histidine
viruses
stems
membrane fusion

ASJC Scopus subject areas

  • Immunology

Cite this

Second-site revertants of a Semliki Forest Virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein. / Chanel-Vos, Chantal; Kielian, Margaret.

In: Journal of Virology, Vol. 80, No. 12, 06.2006, p. 6115-6122.

Research output: Contribution to journalArticle

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