Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G
| Autor: | Derek Odell, Essam Wanas, Hara P. Ghosh, Jesi Yan |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Cytoplasm
Glycosylphosphatidylinositols G protein Recombinant Fusion Proteins Molecular Sequence Data Immunology Golgi Apparatus Biology Endoplasmic Reticulum Transfection Membrane Fusion Microbiology Vesicular stomatitis Indiana virus Cell Line Viral Envelope Proteins Cricetinae Virology Animals Amino Acid Sequence Integral membrane protein Peptide sequence Glycoproteins chemistry.chemical_classification Membrane Glycoproteins Lipid bilayer fusion Hydrogen-Ion Concentration biology.organism_classification Fusion protein Transmembrane protein Cell biology Kinetics Biochemistry chemistry Vesicular stomatitis virus Insect Science CD4 Antigens COS Cells Glycoprotein Research Article |
| Zdroj: | Journal of Virology. 71:7996-8000 |
| ISSN: | 1098-5514 0022-538X |
| Popis: | Chimeric proteins in which the transmembrane anchoring sequence (TM) or both the TM and the cytoplasmic tail (CT) of vesicular stomatitis virus glycoprotein G were replaced with corresponding domains of viral or cellular integral membrane proteins were used to examine the influence of these domains on acidic-pH-induced membrane fusion by G protein. The TM and CT of G were also replaced with the lipid anchor glycosylphosphatidylinositol. Hybrids containing foreign TM or TM and CT sequences were fusogenic at acidic pH but glycosylphosphatidylinositol-anchored G was nonfusogenic at acidic pH. The results suggest that the fusogenic activity of G protein requires membrane anchoring by a hydrophobic peptide sequence and the specific amino acid sequence of the TM has no influence on fusogenic activity. |
| Databáze: | OpenAIRE |
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