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

Maofu Liao, Margaret Kielian

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The alphavirus Semliki Forest virus (SFV) infects cells via a low pH-triggered fusion reaction mediated by the viral E1 protein. Both the E1 fusion peptide and transmembrane (TM) domain are essential for membrane fusion, but the functional requirements for the TM domain are poorly understood. Here we explored the role of the five TM domain glycine residues, including the highly conserved glycine pair at E1 residues 415/416. SFV mutants with alanine substitutions for individual or all five glycine residues (5G/A) showed growth kinetics and fusion pH dependence similar to those of wild-type SFV. Mutants with increasing substitution of glycine residues showed an increasingly more stringent requirement for cholesterol during fusion. The 5G/A mutant showed decreased fusion kinetics and extent in fluorescent lipid mixing assays. TM domain glycine residues thus are not required for efficient SFV fusion or assembly but can cause subtle effects on the properties of membrane fusion.

Original languageEnglish (US)
Pages (from-to)430-437
Number of pages8
JournalVirology
Volume332
Issue number1
DOIs
StatePublished - Feb 5 2005

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Viral Fusion Proteins
Semliki forest virus
Glycine
Membrane Fusion
Alphavirus
Viral Proteins
Alanine
Cholesterol
Lipids
Growth

Keywords

  • Alphavirus
  • Glycine residues
  • Membrane fusion
  • Semliki Forest virus
  • Transmembrane

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases

Cite this

The conserved glycine residues in the transmembrane domain of the Semliki Forest virus fusion protein are not required for assembly and fusion. / Liao, Maofu; Kielian, Margaret.

In: Virology, Vol. 332, No. 1, 05.02.2005, p. 430-437.

Research output: Contribution to journalArticle

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