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_17
Snippet: All of these glycoproteins require proteolytic processing (32, 33) following internalization into the target cell and utilize the lysosomal protein NPC1 to initiate viral fusion (34, 35). In addition to the EBOV and MARV glycoproteins tested in Fig 1A, The copyright holder for this preprint (which was not peer-reviewed) is the author/funder.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 shown in Fig. 1B , none of the filoviral glycopr.....
Document: All of these glycoproteins require proteolytic processing (32, 33) following internalization into the target cell and utilize the lysosomal protein NPC1 to initiate viral fusion (34, 35). In addition to the EBOV and MARV glycoproteins tested in Fig 1A, The copyright holder for this preprint (which was not peer-reviewed) is the author/funder.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 shown in Fig. 1B , none of the filoviral glycoproteins were inhibited >10-fold in the presence of SERINC5. However, there may be modest differences in sensitivity to SERINC5 activity, specifically RESTV and TAFV GP appear slightly more sensitive (4.3-and 2.9-fold, respectively) to SERINC5 inhibition compared to either Mayinga or Makona Ebola virus glycoproteins (1.65-and 1.2-fold, respectively).
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