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An evolving arsenal: viral RNA detection by RIG-I-like receptors

RIG-I-like receptors (RLRs) utilize a specialized, multi-domain architecture to detect and respond to invasion by a diverse set of viruses. Structural similarities among these receptors provide a general mechanism for double strand RNA recognition and signal transduction. However, each RLR has devel...

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Detalles Bibliográficos
Autores principales: Fitzgerald, Megan E, Rawling, David C, Vela, Adriana, Pyle, Anna Marie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7108371/
https://www.ncbi.nlm.nih.gov/pubmed/24912143
http://dx.doi.org/10.1016/j.mib.2014.05.004
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author Fitzgerald, Megan E
Rawling, David C
Vela, Adriana
Pyle, Anna Marie
author_facet Fitzgerald, Megan E
Rawling, David C
Vela, Adriana
Pyle, Anna Marie
author_sort Fitzgerald, Megan E
collection PubMed
description RIG-I-like receptors (RLRs) utilize a specialized, multi-domain architecture to detect and respond to invasion by a diverse set of viruses. Structural similarities among these receptors provide a general mechanism for double strand RNA recognition and signal transduction. However, each RLR has developed unique strategies for sensing the specific molecular determinants on subgroups of viral RNAs. As a means to circumvent the antiviral response, viruses escape RLR detection by degrading, or sequestering or modifying their RNA. Patterns of variation in RLR sequence reveal a continuous evolution of the protein domains that contribute to RNA recognition and signaling.
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spelling pubmed-71083712020-03-31 An evolving arsenal: viral RNA detection by RIG-I-like receptors Fitzgerald, Megan E Rawling, David C Vela, Adriana Pyle, Anna Marie Curr Opin Microbiol Article RIG-I-like receptors (RLRs) utilize a specialized, multi-domain architecture to detect and respond to invasion by a diverse set of viruses. Structural similarities among these receptors provide a general mechanism for double strand RNA recognition and signal transduction. However, each RLR has developed unique strategies for sensing the specific molecular determinants on subgroups of viral RNAs. As a means to circumvent the antiviral response, viruses escape RLR detection by degrading, or sequestering or modifying their RNA. Patterns of variation in RLR sequence reveal a continuous evolution of the protein domains that contribute to RNA recognition and signaling. Elsevier Ltd. 2014-08 2014-06-07 /pmc/articles/PMC7108371/ /pubmed/24912143 http://dx.doi.org/10.1016/j.mib.2014.05.004 Text en Copyright © 2014 Elsevier Ltd. 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
Fitzgerald, Megan E
Rawling, David C
Vela, Adriana
Pyle, Anna Marie
An evolving arsenal: viral RNA detection by RIG-I-like receptors
title An evolving arsenal: viral RNA detection by RIG-I-like receptors
title_full An evolving arsenal: viral RNA detection by RIG-I-like receptors
title_fullStr An evolving arsenal: viral RNA detection by RIG-I-like receptors
title_full_unstemmed An evolving arsenal: viral RNA detection by RIG-I-like receptors
title_short An evolving arsenal: viral RNA detection by RIG-I-like receptors
title_sort evolving arsenal: viral rna detection by rig-i-like receptors
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7108371/
https://www.ncbi.nlm.nih.gov/pubmed/24912143
http://dx.doi.org/10.1016/j.mib.2014.05.004
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