ArticleNucleic acids research2018
The methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 50 citations in OpenAlex.
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- Conserved Filovirus Proteins as Targets of Broad-Spectrum Antivirals.bioRxiv : the preprint server for biology · 2025Article
- The complete pathway for co-transcriptional mRNA maturation within a large protein of a non-segmented negative-strand RNA virus.Nucleic acids research · 2024Article
- How does the polymerase of non-segmented negative strand RNA viruses commit to transcription or genome replication?Journal of virology · 2024Review
- Molecular insights into the Ebola virus life cycle.Nature microbiology · 2024Review
- Coronavirus 2'-O-methyltransferase: A promising therapeutic target.Virus research · 2023Review
- Internal RNA 2'O-methylation in the HIV-1 genome counteracts ISG20 nuclease-mediated antiviral effect.Nucleic acids research · 2023Article
- Biochemistry of the Respiratory Syncytial Virus L Protein Embedding RNA Polymerase and Capping Activities.Viruses · 2023Review
- The regulation of antiviral innate immunity through non-mFrontiers in immunology · 2023Review
- Regulation of antiviral innate immunity by chemical modification of viral RNA.Wiley interdisciplinary reviews. RNA · 2022Review
- A second type of N7-guanine RNA cap methyltransferase in an unusual locus of a large RNA virus genome.Nucleic acids research · 2022Article
- Methyltransferases ofBiomolecules · 2022Article
- DNA Methyltransferases: From Evolution to Clinical Applications.International journal of molecular sciences · 2022Review
- Biochemical and Biophysical Characterisation of the Hepatitis E Virus Guanine-7-Methyltransferase.Molecules (Basel, Switzerland) · 2022Article
- Mutations in the Methyltransferase Motifs of L Protein Attenuate Newcastle Disease Virus by Regulating Viral Translation and Cell-to-Cell Spread.Microbiology spectrum · 2021Article
- Structural and Functional Aspects of Ebola Virus Proteins.Pathogens (Basel, Switzerland) · 2021Review
- 2'-O methylation of RNA cap in SARS-CoV-2 captured by serial crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The methyltransferase domain of the Respiratory Syncytial Virus L protein catalyzes cap N7 and 2'-O-methylation.PLoS pathogens · 2021Article
- Flipping the script: viral capitalization of RNA modifications.Briefings in functional genomics · 2021Review
- First insights into the structural features of Ebola virus methyltransferase activities.Nucleic acids research · 2021Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Mononegaviruses, such as Ebola virus, encode an L (large) protein that bears all the catalytic activities for replication/transcription and RNA capping. The C-terminal conserved region VI (CRVI) of L protein contains a K-D-K-E catalytic tetrad typical for 2'O methyltransferases (MTase). In mononegaviruses, cap-MTase activities have been involved in the 2'O methylation and N7 methylation of the RNA cap structure. These activities play a critical role in the viral life cycle as N7 methylation ensures efficient viral mRNA translation and 2'O methylation hampers the detection of viral RNA by the host innate immunity. The functional characterization of the MTase+CTD domain of Sudan ebolavirus (SUDV) revealed cap-independent methyltransferase activities targeting internal adenosine residues. Besides this, the MTase+CTD also methylates, the N7 position of the cap guanosine and the 2'O position of the n1 guanosine provided that the RNA is sufficiently long. Altogether, these results suggest that the filovirus MTases evolved towards a dual activity with distinct substrate specificities. Whereas it has been well established that cap-dependent methylations promote protein translation and help to mimic host RNA, the characterization of an original cap-independent methylation opens new research opportunities to elucidate the role of RNA internal methylations in the viral replication.
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