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First insights into the structural features of Ebola virus methyltransferase activities

Abstract : The Ebola virus is a deadly human pathogen responsible for several outbreaks in Africa. Its genome encodes the 'large' L protein, an essential enzyme that has polymerase, capping and methyltransferase activities. The methyltransferase activity leads to RNA co-transcriptional modifications at the N7 position of the cap structure and at the 2-O position of the first transcribed nucleotide. Unlike other Mononegavirales viruses, the Ebola virus methyltransferase also catalyses 2-O-methylation of adenosines located within the RNA sequences. Herein, we report the crystal structure at 1.8Å resolution of the Ebola virus methyltransferase domain bound to a fragment of a camelid single-chain antibody. We identified structural determinants and key amino acids specifically involved in the internal adenosine-2-Omethylation from cap-related methylations. These results provide the first high resolution structure of an ebolavirus L protein domain, and the framework to investigate the effects of epitranscriptomic modifications and to design possible antiviral drugs against the Filoviridae family.
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https://hal.archives-ouvertes.fr/hal-03334409
Contributor : Jean-Jacques Vasseur Connect in order to contact the contributor
Submitted on : Friday, September 3, 2021 - 4:59:27 PM
Last modification on : Wednesday, January 19, 2022 - 4:58:50 PM
Long-term archiving on: : Saturday, December 4, 2021 - 8:01:47 PM

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Coralie Valle, Baptiste Martin, François Ferron, Véronique Roig-Zamboni, Aline Desmyter, et al.. First insights into the structural features of Ebola virus methyltransferase activities. Nucleic Acids Research, Oxford University Press, 2021, 49 (3), pp.1737 - 1748. ⟨10.1093/nar/gkaa1276⟩. ⟨hal-03334409⟩

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