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_8
Snippet: SERINC5 is a multipass transmembrane that localizes almost exclusively to the plasma membrane (17, 18) . As such, in the absence of counter-measures, all enveloped viruses would be expected to encounter SERINC5 during viral egress, and to potentially be subject to its antiviral effects. We sought to address the breadth of SERINC5 antiviral activity and assess whether the route of entry impacts the sensitivity of viral glycoproteins to the antivir.....
Document: SERINC5 is a multipass transmembrane that localizes almost exclusively to the plasma membrane (17, 18) . As such, in the absence of counter-measures, all enveloped viruses would be expected to encounter SERINC5 during viral egress, and to potentially be subject to its antiviral effects. We sought to address the breadth of SERINC5 antiviral activity and assess whether the route of entry impacts the sensitivity of viral glycoproteins to the antiviral effects of SERINC5. To do so, we investigated whether the co-expression of SERINC5 during viral production could inhibit a variety of glycoprotein pseudotypes of HIV, MLV, or M-PMV cores.
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