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Inhibition of the OAS/RNase L pathway by viruses

The OAS/RNase L system was one of the first characterized interferon effector pathways. It relies on the synthesis, by oligoadenylate synthetases (OAS), of short oligonucleotides that act as second messengers to activate the latent cellular RNase L. Viruses have developed diverse strategies to escap...

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Detalles Bibliográficos
Autores principales: Drappier, Melissa, Michiels, Thomas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7185432/
https://www.ncbi.nlm.nih.gov/pubmed/26231767
http://dx.doi.org/10.1016/j.coviro.2015.07.002
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author Drappier, Melissa
Michiels, Thomas
author_facet Drappier, Melissa
Michiels, Thomas
author_sort Drappier, Melissa
collection PubMed
description The OAS/RNase L system was one of the first characterized interferon effector pathways. It relies on the synthesis, by oligoadenylate synthetases (OAS), of short oligonucleotides that act as second messengers to activate the latent cellular RNase L. Viruses have developed diverse strategies to escape its antiviral effects. This underscores the importance of the OAS/RNase L pathway in antiviral defenses. Viral proteins such as the NS1 protein of Influenza virus A act upstream of the pathway while other viral proteins such as Theiler's virus L* protein act downstream. The diversity of escape strategies used by viruses likely stems from their relative susceptibility to OAS/RNase L and other antiviral pathways, which may depend on their host and cellular tropism.
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spelling pubmed-71854322020-04-28 Inhibition of the OAS/RNase L pathway by viruses Drappier, Melissa Michiels, Thomas Curr Opin Virol Article The OAS/RNase L system was one of the first characterized interferon effector pathways. It relies on the synthesis, by oligoadenylate synthetases (OAS), of short oligonucleotides that act as second messengers to activate the latent cellular RNase L. Viruses have developed diverse strategies to escape its antiviral effects. This underscores the importance of the OAS/RNase L pathway in antiviral defenses. Viral proteins such as the NS1 protein of Influenza virus A act upstream of the pathway while other viral proteins such as Theiler's virus L* protein act downstream. The diversity of escape strategies used by viruses likely stems from their relative susceptibility to OAS/RNase L and other antiviral pathways, which may depend on their host and cellular tropism. Elsevier B.V. 2015-12 2015-07-29 /pmc/articles/PMC7185432/ /pubmed/26231767 http://dx.doi.org/10.1016/j.coviro.2015.07.002 Text en Copyright © 2015 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Drappier, Melissa
Michiels, Thomas
Inhibition of the OAS/RNase L pathway by viruses
title Inhibition of the OAS/RNase L pathway by viruses
title_full Inhibition of the OAS/RNase L pathway by viruses
title_fullStr Inhibition of the OAS/RNase L pathway by viruses
title_full_unstemmed Inhibition of the OAS/RNase L pathway by viruses
title_short Inhibition of the OAS/RNase L pathway by viruses
title_sort inhibition of the oas/rnase l pathway by viruses
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7185432/
https://www.ncbi.nlm.nih.gov/pubmed/26231767
http://dx.doi.org/10.1016/j.coviro.2015.07.002
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