RIG-I and dsRNA-induced IFNbeta activation.

Except for viruses that initiate RNA synthesis with a protein primer (e.g., picornaviruses), most RNA viruses initiate RNA synthesis with an NTP, and at least some of their viral (ppp)RNAs remain unblocked during the infection. Consistent with this, most viruses require RIG-I to mount an innate immu...

Full description

Bibliographic Details
Main Authors: Stéphane Hausmann, Jean-Baptiste Marq, Caroline Tapparel, Daniel Kolakofsky, Dominique Garcin
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2008-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2607022?pdf=render
id doaj-3f76c757d86644fd9f330466bbae2d1b
record_format Article
spelling doaj-3f76c757d86644fd9f330466bbae2d1b2020-11-24T22:06:49ZengPublic Library of Science (PLoS)PLoS ONE1932-62032008-01-01312e396510.1371/journal.pone.0003965RIG-I and dsRNA-induced IFNbeta activation.Stéphane HausmannJean-Baptiste MarqCaroline TapparelDaniel KolakofskyDominique GarcinExcept for viruses that initiate RNA synthesis with a protein primer (e.g., picornaviruses), most RNA viruses initiate RNA synthesis with an NTP, and at least some of their viral (ppp)RNAs remain unblocked during the infection. Consistent with this, most viruses require RIG-I to mount an innate immune response, whereas picornaviruses require mda-5. We have examined a SeV infection whose ability to induce interferon depends on the generation of capped dsRNA (without free 5' tri-phosphate ends), and found that this infection as well requires RIG-I and not mda-5. We also provide evidence that RIG-I interacts with poly-I/C in vivo, and that heteropolymeric dsRNA and poly-I/C interact directly with RIG-I in vitro, but in different ways; i.e., poly-I/C has the unique ability to stimulate the helicase ATPase of RIG-I variants which lack the C-terminal regulatory domain.http://europepmc.org/articles/PMC2607022?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Stéphane Hausmann
Jean-Baptiste Marq
Caroline Tapparel
Daniel Kolakofsky
Dominique Garcin
spellingShingle Stéphane Hausmann
Jean-Baptiste Marq
Caroline Tapparel
Daniel Kolakofsky
Dominique Garcin
RIG-I and dsRNA-induced IFNbeta activation.
PLoS ONE
author_facet Stéphane Hausmann
Jean-Baptiste Marq
Caroline Tapparel
Daniel Kolakofsky
Dominique Garcin
author_sort Stéphane Hausmann
title RIG-I and dsRNA-induced IFNbeta activation.
title_short RIG-I and dsRNA-induced IFNbeta activation.
title_full RIG-I and dsRNA-induced IFNbeta activation.
title_fullStr RIG-I and dsRNA-induced IFNbeta activation.
title_full_unstemmed RIG-I and dsRNA-induced IFNbeta activation.
title_sort rig-i and dsrna-induced ifnbeta activation.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2008-01-01
description Except for viruses that initiate RNA synthesis with a protein primer (e.g., picornaviruses), most RNA viruses initiate RNA synthesis with an NTP, and at least some of their viral (ppp)RNAs remain unblocked during the infection. Consistent with this, most viruses require RIG-I to mount an innate immune response, whereas picornaviruses require mda-5. We have examined a SeV infection whose ability to induce interferon depends on the generation of capped dsRNA (without free 5' tri-phosphate ends), and found that this infection as well requires RIG-I and not mda-5. We also provide evidence that RIG-I interacts with poly-I/C in vivo, and that heteropolymeric dsRNA and poly-I/C interact directly with RIG-I in vitro, but in different ways; i.e., poly-I/C has the unique ability to stimulate the helicase ATPase of RIG-I variants which lack the C-terminal regulatory domain.
url http://europepmc.org/articles/PMC2607022?pdf=render
work_keys_str_mv AT stephanehausmann rigianddsrnainducedifnbetaactivation
AT jeanbaptistemarq rigianddsrnainducedifnbetaactivation
AT carolinetapparel rigianddsrnainducedifnbetaactivation
AT danielkolakofsky rigianddsrnainducedifnbetaactivation
AT dominiquegarcin rigianddsrnainducedifnbetaactivation
_version_ 1725821641658728448