Author: Martin, Baptiste; Coutard, Bruno; Guez, Théo; Paesen, Guido C; Canard, Bruno; Debart, Françoise; Vasseur, Jean-Jacques; Grimes, Jonathan M; Decroly, Etienne
Title: The methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure Document date: 2018_9_6
ID: 243u68j8_32
Snippet: To date, there are few structural or biochemical data on the Ebola virus L protein, which compromises our understanding of the viral replication/transcription mechanisms and development of inhibitors with potential antiviral effect. In this study, we produced and purified the C-terminal region of the SUDV L protein encompassing the MTase and CTD domains (MTase+CTD). The functional study of this protein leads to the discovery of three MTase activi.....
Document: To date, there are few structural or biochemical data on the Ebola virus L protein, which compromises our understanding of the viral replication/transcription mechanisms and development of inhibitors with potential antiviral effect. In this study, we produced and purified the C-terminal region of the SUDV L protein encompassing the MTase and CTD domains (MTase+CTD). The functional study of this protein leads to the discovery of three MTase activities allowing the N7 and 2'O methylations of RNA cap structure and 2'O methylation of internal adenosines within RNA. Internal A-2'O MTase activity has not yet been reported in Mononegavirales in contrast to flaviviruses (29, 34) with a putative biological role on virus replication, transcription.
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