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Molecular characterisation of RIG-I-like helicases in the black flying fox, Pteropus alecto
The RIG-I like helicases, RIG-I, mda5 and LGP2 are an evolutionarily conserved family of cytosolic pattern recognition receptors important in the recognition of viral RNA, and responsible for the innate induction of interferons and proinflammatory cytokines upon viral infection. Bats are natural res...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Elsevier Ltd.
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103216/ https://www.ncbi.nlm.nih.gov/pubmed/22166340 http://dx.doi.org/10.1016/j.dci.2011.11.008 |
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author | Cowled, Christopher Baker, Michelle L. Zhou, Peng Tachedjian, Mary Wang, Lin-Fa |
author_facet | Cowled, Christopher Baker, Michelle L. Zhou, Peng Tachedjian, Mary Wang, Lin-Fa |
author_sort | Cowled, Christopher |
collection | PubMed |
description | The RIG-I like helicases, RIG-I, mda5 and LGP2 are an evolutionarily conserved family of cytosolic pattern recognition receptors important in the recognition of viral RNA, and responsible for the innate induction of interferons and proinflammatory cytokines upon viral infection. Bats are natural reservoir hosts to a variety of RNA viruses that cause significant morbidity and mortality in other species; however the mechanisms responsible for the control of viral replication in bats are not understood. This report describes the molecular cloning and expression analysis of RIG-I, mda5 and LGP2 genes in the fruit bat Pteropus alecto, and is the first description of RIG-I like helicases from any species of bat. Our results demonstrate that P. alecto RIG-I, mda5 and LGP2 have similar primary structures and tissue expression patterns to their counterparts in humans and other mammals. Stimulation of bat kidney cells with synthetic dsRNA (poly I:C) induced high levels of interferon β and rapid upregulation of all three helicases. These findings reveal that the cytoplasmic virus sensing machinery is present and intact in P. alecto. This study provides the foundation for further investigations into the interactions between bat RIG-I-like helicases and viruses to elucidate the mechanisms responsible for the asymptomatic nature of viral infections in bats. |
format | Online Article Text |
id | pubmed-7103216 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Published by Elsevier Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71032162020-03-31 Molecular characterisation of RIG-I-like helicases in the black flying fox, Pteropus alecto Cowled, Christopher Baker, Michelle L. Zhou, Peng Tachedjian, Mary Wang, Lin-Fa Dev Comp Immunol Article The RIG-I like helicases, RIG-I, mda5 and LGP2 are an evolutionarily conserved family of cytosolic pattern recognition receptors important in the recognition of viral RNA, and responsible for the innate induction of interferons and proinflammatory cytokines upon viral infection. Bats are natural reservoir hosts to a variety of RNA viruses that cause significant morbidity and mortality in other species; however the mechanisms responsible for the control of viral replication in bats are not understood. This report describes the molecular cloning and expression analysis of RIG-I, mda5 and LGP2 genes in the fruit bat Pteropus alecto, and is the first description of RIG-I like helicases from any species of bat. Our results demonstrate that P. alecto RIG-I, mda5 and LGP2 have similar primary structures and tissue expression patterns to their counterparts in humans and other mammals. Stimulation of bat kidney cells with synthetic dsRNA (poly I:C) induced high levels of interferon β and rapid upregulation of all three helicases. These findings reveal that the cytoplasmic virus sensing machinery is present and intact in P. alecto. This study provides the foundation for further investigations into the interactions between bat RIG-I-like helicases and viruses to elucidate the mechanisms responsible for the asymptomatic nature of viral infections in bats. Published by Elsevier Ltd. 2012-04 2011-12-03 /pmc/articles/PMC7103216/ /pubmed/22166340 http://dx.doi.org/10.1016/j.dci.2011.11.008 Text en Crown copyright © 2011 Published by 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 Cowled, Christopher Baker, Michelle L. Zhou, Peng Tachedjian, Mary Wang, Lin-Fa Molecular characterisation of RIG-I-like helicases in the black flying fox, Pteropus alecto |
title | Molecular characterisation of RIG-I-like helicases in the black flying fox, Pteropus alecto |
title_full | Molecular characterisation of RIG-I-like helicases in the black flying fox, Pteropus alecto |
title_fullStr | Molecular characterisation of RIG-I-like helicases in the black flying fox, Pteropus alecto |
title_full_unstemmed | Molecular characterisation of RIG-I-like helicases in the black flying fox, Pteropus alecto |
title_short | Molecular characterisation of RIG-I-like helicases in the black flying fox, Pteropus alecto |
title_sort | molecular characterisation of rig-i-like helicases in the black flying fox, pteropus alecto |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103216/ https://www.ncbi.nlm.nih.gov/pubmed/22166340 http://dx.doi.org/10.1016/j.dci.2011.11.008 |
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