Author: Aravinth Kumar Jayabalan; Diane E. Griffin; Anthony K. L. Leung
Title: Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation Document date: 2019_6_20
ID: n8sjpcbs_22
Snippet: To determine whether the observed role of nsP3 MD ADP-ribosylhydrolase activity during arsenite-induced stress is relevant in a physiological context, we tested whether MD hydrolase mutation affects SG assembly in CHIKV-infected cells. Given that CHIKVs with nsP3 mutations (D10A, G32E, G112E) that severely compromise ADP-ribose binding and hydrolase activities are not viable [38] , we focused on viable CHIKV mutants G32S and Y114A with diminished.....
Document: To determine whether the observed role of nsP3 MD ADP-ribosylhydrolase activity during arsenite-induced stress is relevant in a physiological context, we tested whether MD hydrolase mutation affects SG assembly in CHIKV-infected cells. Given that CHIKVs with nsP3 mutations (D10A, G32E, G112E) that severely compromise ADP-ribose binding and hydrolase activities are not viable [38] , we focused on viable CHIKV mutants G32S and Y114A with diminished, but not absent, hydrolase activity.
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