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Virology. 1999 Mar 30;256(1):119-29.

Effects of double-site mutations of vesicular stomatitis virus glycoprotein G on membrane fusion activity.

Author information

1
Department of Biochemistry, McMaster University, Hamilton, Ontario, L8N 3Z5, Canada.

Abstract

Site-directed mutagenesis of specific amino acids within a conserved amino-terminal region (H2) and a conserved carboxyl-terminal region (H10/A4) of the fusion protein G of vesicular stomatitis virus have previously identified these two segments as an internal fusion peptide and a region influencing low-pH induced conformational change, respectively. Here, we combined a number of the substitution mutants in the H2 and H10/A4 regions to produce a series of double-site mutants and determined the effect of these mutations on membrane fusion activity at acid pH and on pH-dependent conformational change. The results show that most of the double-site mutants have decreased cell-cell fusion activity and that the effects appeared to be additive in terms of inhibition of fusion, except for one mutant, which appeared to be a revertant. The double-site mutants also had pH optima for fusion that were lower than those observed with wild-type G but same as the pH optima for the parent fusion peptide (H2) mutants. The results suggest that although the H2 and H10/A4 sites may affect membrane fusion independently, a possible interaction between these two sites cannot be ruled out.

PMID:
10087232
DOI:
10.1006/viro.1999.9606
[Indexed for MEDLINE]
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