Effects of Double-Site Mutations of Vesicular Stomatitis Virus Glycoprotein G on Membrane Fusion Activity
| Autor: | Robert Chernish, Shahira Shokralla, Hara P. Ghosh |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Conformational change
Protein Conformation Mutant Mutagenesis (molecular biology technique) Biology Transfection Membrane Fusion Vesicular stomatitis Indiana virus Cell Fusion Viral Envelope Proteins Virology Animals Amino Acid Sequence Conserved Sequence chemistry.chemical_classification Membrane Glycoproteins Lipid bilayer fusion biology.organism_classification Fusion protein Recombinant Proteins Amino acid Amino Acid Substitution chemistry Biochemistry Vesicular stomatitis virus COS Cells Mutagenesis Site-Directed Membrane Fusion Activity |
| Zdroj: | Virology. 256:119-129 |
| ISSN: | 0042-6822 |
| DOI: | 10.1006/viro.1999.9606 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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