Semliki Forest virus produced in the absence of the 6K protein has an altered spike structure as revealed by decreased membrane fusion capacity

Virology
Gerald M McInerneyJan Wilschut

Abstract

We examined the kinetics of membrane fusion of wild type (wt) and Delta6K mutant Semliki Forest virus in a liposomal model system. The final extent of membrane fusion of the mutant (at pH 5.5) was approximately one third that of the wt virus, although the level of E1 (fusion protein) trimerization was, in fact, greater than that of the wt. Studies on the effect of exposure of the viruses to low pH revealed that the Delta6K mutant was inactivated much more rapidly than the wt virus. It is this instability of the mutant particles which probably accounts for the lower fusion levels. Moreover, fusion of the Delta6K mutant was significantly increased by the inclusion of lipid-conjugated heparin in the target liposomes. We conclude that the presence of the 6K protein either in the particle or during the assembly process is important for the correct assembly of the fully infectious SFV particle.

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Citations

Sep 3, 2009·Future Microbiology·Joyce JoseRichard J Kuhn
May 28, 2005·Journal of Virology·Barry-Lee WaartsJan Wilschut
Jan 19, 2007·Molecular Biology of the Cell·Tamar GattegnoBenjamin Podbilewicz
Sep 30, 2008·Virology Journal·Andrew E FirthJohn F Atkins
May 31, 2013·Journal of Virology·Jonathan E SnyderRichard J Kuhn
Apr 6, 2005·The Journal of Cell Biology·Elena ZaitsevaLeonid V Chernomordik
Jun 21, 2005·FEBS Letters·Vanessa MadanLuis Carrasco
May 30, 2015·The Journal of General Virology·Claire Scott, Stephen Griffin
Mar 26, 2010·Viruses·Margaret KielianMaofu Liao
Aug 19, 2017·Viruses·Jolene Ramsey, Suchetana Mukhopadhyay
Feb 13, 2016·Journal of Virology·Adam TaylorSuresh Mahalingam
Jan 13, 2012·Journal of Virology·Anthony J SnyderSuchetana Mukhopadhyay
Nov 5, 2021·Journal of Medical Entomology·Alexander T Ciota

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