The Fusion Glycoprotein Shell of Semliki Forest Virus
| Autor: | Jorge Navaza, Gerd Wengler, Julien Lescar, Stephen D. Fuller, Félix A. Rey, Gisela Wengler, Michelle W. Wien, Alain Roussel |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Biochemistry Genetics and Molecular Biology(all) Endosome Viral protein viruses 030302 biochemistry & molecular biology Lipid bilayer fusion biochemical phenomena metabolism and nutrition Biology Semliki Forest virus biology.organism_classification medicine.disease_cause General Biochemistry Genetics and Molecular Biology Virus 03 medical and health sciences Flavivirus Biochemistry chemistry Viral envelope Biophysics medicine Glycoprotein 030304 developmental biology |
| Zdroj: | Cell. 105:137-148 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/s0092-8674(01)00303-8 |
| Popis: | Semliki Forest virus (SFV) has been extensively studied as a model for analyzing entry of enveloped viruses into target cells. Here we describe the trace of the polypeptide chain of the SFV fusion glycoprotein, E1, derived from an electron density map at 3.5 A resolution and describe its interactions at the surface of the virus. E1 is unexpectedly similar to the flavivirus envelope protein, with three structural domains disposed in the same primary sequence arrangement. These results introduce a new class of membrane fusion proteins which display lateral interactions to induce the necessary curvature and direct budding of closed particles. The resulting surface protein lattice is primed to cause membrane fusion when exposed to the acidic environment of the endosome. |
| Databáze: | OpenAIRE |
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