pntd.0008283.g007.tif (1.05 MB)
Download fileQualitative analysis of polyUb chain hydrolysis by CCHFV L protein and the isolated CCHFV OTU domain.
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posted on 04.06.2020, 17:28 authored by Egor P. Tchesnokov, Ben A. Bailey-Elkin, Brian L. Mark, Matthias GöttePurified CCHFV L protein (RdRp) was incubated with either (A) K48polyUb or (B) K63polyUb chains in the presence or absence of OTU-specific inhibitor CC.4. Ub chain hydrolysis was also assessed for the purified OTU domain using (C) K48polyUb chains or (D) K63polyUb chains in the presence or absence of CC.4. Reactions were incubated at 37°C and samples taken at 0, 15 and 30 minutes as indicated. Ub chain lengths following digestion are indicated with arrows. Samples were resolved on a 10% tris-tricine gel and visualized by silver stain.
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World Health OrganizationRNA synthesisCrimean-Congo hemorrhagic fever virusbroad-spectrum antivirals ribavirinD 2517N mutationlength RNA productCrimean-Congo Hemorrhagic Fever VirusRNA-dependent RNA polymerasemultifunctional L proteinHTSubiquitin analogue CCATPLys 63-linked polyubiqutin chainsCCHFV L proteinGTPCCHFV L-proteinCCHFV-associated DUB activitydivalent metal ionsDUB activitynegative-sense RNA virusCCHFV RdRp activityOTU