Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane
| Autor: | Romke Bron, Jan Wilschut, José Luis Nieva, Jeroen Corver |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Ceramide
Endosome viruses Ceramides Semliki Forest virus Membrane Fusion General Biochemistry Genetics and Molecular Biology Structure-Activity Relationship chemistry.chemical_compound Viral envelope Molecular Biology Sphingolipids General Immunology and Microbiology biology General Neuroscience Fatty Acids Lipid bilayer fusion Hydrogen-Ion Concentration biochemical phenomena metabolism and nutrition biology.organism_classification Semliki forest virus Fusion protein Sphingolipid Cell biology Cholesterol chemistry Biochemistry Liposomes lipids (amino acids peptides and proteins) Sphingomyelin Acids Research Article |
| Zdroj: | The EMBO Journal. 13:2797-2804 |
| ISSN: | 0261-4189 |
| Popis: | Enveloped animal viruses, such as Semliki Forest virus (SFV), utilize a membrane fusion strategy to deposit their genome into the cytosol of the host cell. SFV enters cells through receptor-mediated endocytosis, fusion of the viral envelope occurring subsequently from within acidic endosomes. Fusion of SFV has been demonstrated before to be strictly dependent on the presence of cholesterol in the target membrane. Here, utilizing a variety of membrane fusion assays, including an on-line fluorescence assay involving pyrene-labeled virus, we demonstrate that low-pH-induced fusion of SFV with cholesterol-containing liposomal model membranes requires the presence of sphingomyelin or other sphingolipids in the target membrane. The minimal molecular characteristics essential for supporting SFV fusion are encompassed by a ceramide. The action of the sphingolipids is confined to the actual fusion event, cholesterol being necessary and sufficient for low-pH-dependent binding of the virus to target membranes. Complex formation of the sphingolipids with cholesterol is unlikely to be important for the induction of SFV--liposome fusion, as sphingolipids that do not interact appreciably with cholesterol, such as galactosylceramide, effectively support the process. The remarkably low levels of sphingomyelin required for half-maximal fusion (1-2 mole%) suggest that sphingolipids do not play a structural role in the SFV fusion process, but rather act as a cofactor, possibly activating the viral fusion protein in a specific manner. |
| Databáze: | OpenAIRE |
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