VSV-G
VSV glycoprotein | ||
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other names |
VSV-G |
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Mass / length primary structure | 517 amino acids , 58,230 Da | |
Secondary to quaternary structure | homotrimer | |
Identifier | ||
External IDs |
The VSV-G is a glycoprotein from the Vesicular stomatitis virus (VSV).
properties
The VSV-G is the homotrimeric receptor in the virus envelope of the virus with a comparatively wide tropism . It's the peplomer in the virus envelope. After the VSV-G binds to the cell surface, clathrin-mediated endocytosis of the virion into an endosome takes place . Furthermore, VSV-G is a class III fusogenic protein , because after acidification of the endosome a conformational change occurs , whereupon the endosome membrane is penetrated and the inside of the virus is released into the cytosol . In neurons , VSV-G is located in the dendrites , where budding takes place to release newly formed virions.
Applications
VSV-G becomes the pseudo-typing of viral vectors used.
Web links
Individual evidence
- ^ E. Hastie, M. Cataldi, I. Marriott, VZ Grdzelishvili: Understanding and altering cell tropism of vesicular stomatitis virus. In: Virus research. Volume 176, number 1–2, September 2013, pp. 16–32, doi : 10.1016 / j.virusres.2013.06.003 , PMID 23796410 , PMC 3865924 (free full text).
- ↑ J. Cronin, XY Zhang, J. Reiser: Altering the tropism of lentiviral vectors through pseudotyping. In: Current gene therapy. Volume 5, Number 4, August 2005, pp. 387-398, PMID 16101513 , PMC 1368960 (free full text).
- ^ RJ Eisenberg, D. Atanasiu, TM Cairns, JR Gallagher, C. Krummenacher, GH Cohen: Herpes virus fusion and entry: a story with many characters. In: Viruses. Volume 4, number 5, May 2012, pp. 800-832, doi : 10.3390 / v4050800 , PMID 22754650 , PMC 3386629 (free full text).
- ↑ C. Lévy, E. Verhoeyen, FL Cosset: Surface engineering of lentiviral vectors for gene transfer into gene therapy target cells. In: Current opinion in pharmacology. Volume 24, October 2015, pp. 79-85, doi : 10.1016 / j.coph.2015.08.003 , PMID 26298515 .