Author: William E. Diehl; Mehmet H. Guney; Pyae Phyo Kyawe; Judith M. White; Massimo Pizzato; Jeremy Luban
Title: Influence of different glycoproteins and of the virion core on SERINC5 antiviral activity Document date: 2019_9_24
ID: 9dybtdi2_7
Snippet: Importantly, HIV-1 particles pseudotyped with vesicular stomatitis virus (VSV) G or Ebola virus glycoprotein are resistant to SERINC5 antiviral activity (17, 18, 24) . These initial observations suggest a correlation between the location of viral fusion and sensitivity to SERINC5 activity, with glycoproteins that mediate fusion at the cell surface (Env from HIV-1 and amphotropic MLV [A-MLV]) being sensitive and those that mediate fusion in endo-l.....
Document: Importantly, HIV-1 particles pseudotyped with vesicular stomatitis virus (VSV) G or Ebola virus glycoprotein are resistant to SERINC5 antiviral activity (17, 18, 24) . These initial observations suggest a correlation between the location of viral fusion and sensitivity to SERINC5 activity, with glycoproteins that mediate fusion at the cell surface (Env from HIV-1 and amphotropic MLV [A-MLV]) being sensitive and those that mediate fusion in endo-lysosomal compartments . CC-BY-NC-ND 4.0 International license is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It . https://doi.org/10.1101/780577 doi: bioRxiv preprint (VSV-G and Ebola GP) being resistant (17, 24) . Taken together these results indicate that the virion glycoprotein is a viral determinant of sensitivity to SERINC5.
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