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_38
Snippet: The function of such internal A-2'O methylations is not yet understood. Functional analysis using a flavivirus replicon showed that internal methylations attenuate viral RNA replication in BHK-21 cell lines (34) . In addition, internal A-2'O methylations may reduce the efficiency of polymerisation in an in vitro RNA elongation assay (34) . On the other hand, it is also possible that epigenetic/epitranscriptomic RNA modifications increase viral re.....
Document: The function of such internal A-2'O methylations is not yet understood. Functional analysis using a flavivirus replicon showed that internal methylations attenuate viral RNA replication in BHK-21 cell lines (34) . In addition, internal A-2'O methylations may reduce the efficiency of polymerisation in an in vitro RNA elongation assay (34) . On the other hand, it is also possible that epigenetic/epitranscriptomic RNA modifications increase viral replication by limiting the detection of viral RNAs by intracellular sensors and/or restriction factors. Indeed, methylations contribute to structural diversity of RNAs and thus regulate recognition by host proteins (54) . One other possibility is that internal A-2'O methylations would regulate encapsidation. In mononegaviruses, genomic and anti-genomic RNAs are encapsidated by a nucleoprotein (NP) but not mRNAs. Structural work (55) has shown that NP/RNA interactions involve 2'OH groups on the nucleotides. Internal methylation of these groups may thus help NP to discriminate mRNAs from genomic and antigenomic RNAs.
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