La protéine L du virus Ébola porte une nouvelle activité enzymatique impliquée dans la méthylation interne des ARN

Baptiste Martin; Coralie Valle; Bruno Coutard; Bruno Canard; Françoise Debart; Étienne Decroly

doi:10.1051/medsci/2018230

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Volume 34 / Numéro 11 (Novembre 2018)

Med Sci (Paris), 34 11 (2018) 919-921

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Numéro		Med Sci (Paris) Volume 34, Numéro 11, Novembre 2018


Page(s)		919 - 921
Section		Le Magazine
DOI		https://doi.org/10.1051/medsci/2018230
Publié en ligne		10 décembre 2018

Shultz JM, Espinel Z, Espinola M, et al. Distinguishing epidemiological features of the 2013–2016 West Africa Ebola virus disease outbreak. Disaster Heal 2016 ; 3 : 78–88. [CrossRef] [Google Scholar]
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Daffis S, Szretter KJ, Schriewer J, et al. 2’-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature 2010 ; 468 : 452–456. [CrossRef] [PubMed] [Google Scholar]
Paesen GC, Collet A, Sallamand C, et al. X-ray structure and activities of an essential Mononegavirales L-protein domain. Nat. Commun 2015 ; 6 : 8749. [CrossRef] [PubMed] [Google Scholar]
Martin B, Coutard B, Guez T et al. The methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure. Nucl Acids Res 2018; https://doi.org/10.1093/nar/gky637. [Google Scholar]
Coutard B, Barral K, Lichière J, et al. Zika virus methyltransferase: structure and functions for drug design perspectives. J Virol 2017 ; 91 : 5 e02202–e02216. [PubMed] [Google Scholar]
McIntyre W, Netzband R, Bonenfant G, et al. Positive-sense RNA viruses reveal the complexity and dynamics of the cellular and viral epitranscriptomes during infection. Nucleic Acids Res 2018 ; 46 : 5776–5791. [PubMed] [Google Scholar]

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[1] Shultz JM, Espinel Z, Espinola M, et al. Distinguishing epidemiological features of the 2013–2016 West Africa Ebola virus disease outbreak. Disaster Heal 2016 ; 3 : 78–88. [CrossRef] [Google Scholar]

[2] Martin B, Decroly E. Mécanisme d’échappement des filovirus à l’immunité innée. Med Sci (Paris) 2018 ; 34 : 671–677. [CrossRef] [EDP Sciences] [PubMed] [Google Scholar]

[3] Martin B, Canard B, Decroly E. Filovirus proteins for antiviral drug discovery: Structure/function bases of the replication cycle. Antiviral Res 2017 ; 141 : 48–61. [CrossRef] [PubMed] [Google Scholar]

[4] Liang B, Li Z, Jenni S, et al. Structure of the L protein of vesicular stomatitis vrus from electron cryomicroscopy. Cell 2015 ; 162 : 314–327. [CrossRef] [PubMed] [Google Scholar]

[5] Decroly E, Ferron F, Lescar J, et al. Conventional and unconventional mechanisms for capping viral mRNA. Nat Rev Microbiol 2011 ; 10 : 51–65. [CrossRef] [PubMed] [Google Scholar]

[6] Zust R, Cervantes-Barragan L, Habjan M, et al. Ribose 2’-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5. Nat Immunol 2011 ; 12 : 137–143. [CrossRef] [PubMed] [Google Scholar]

[7] Daffis S, Szretter KJ, Schriewer J, et al. 2’-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature 2010 ; 468 : 452–456. [CrossRef] [PubMed] [Google Scholar]

[8] Paesen GC, Collet A, Sallamand C, et al. X-ray structure and activities of an essential Mononegavirales L-protein domain. Nat. Commun 2015 ; 6 : 8749. [CrossRef] [PubMed] [Google Scholar]

[9] Martin B, Coutard B, Guez T et al. The methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure. Nucl Acids Res 2018; https://doi.org/10.1093/nar/gky637. [Google Scholar]

[10] Coutard B, Barral K, Lichière J, et al. Zika virus methyltransferase: structure and functions for drug design perspectives. J Virol 2017 ; 91 : 5 e02202–e02216. [PubMed] [Google Scholar]

[11] McIntyre W, Netzband R, Bonenfant G, et al. Positive-sense RNA viruses reveal the complexity and dynamics of the cellular and viral epitranscriptomes during infection. Nucleic Acids Res 2018 ; 46 : 5776–5791. [PubMed] [Google Scholar]