author_facet Wang, Dang
Fang, Liurong
Wei, Dahai
Zhang, Huan
Luo, Rui
Chen, Huanchun
Li, Kui
Xiao, Shaobo
Wang, Dang
Fang, Liurong
Wei, Dahai
Zhang, Huan
Luo, Rui
Chen, Huanchun
Li, Kui
Xiao, Shaobo
author Wang, Dang
Fang, Liurong
Wei, Dahai
Zhang, Huan
Luo, Rui
Chen, Huanchun
Li, Kui
Xiao, Shaobo
spellingShingle Wang, Dang
Fang, Liurong
Wei, Dahai
Zhang, Huan
Luo, Rui
Chen, Huanchun
Li, Kui
Xiao, Shaobo
Journal of Virology
Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
Virology
Insect Science
Immunology
Microbiology
author_sort wang, dang
spelling Wang, Dang Fang, Liurong Wei, Dahai Zhang, Huan Luo, Rui Chen, Huanchun Li, Kui Xiao, Shaobo 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.00869-14 <jats:title>ABSTRACT</jats:title> <jats:p> NEMO (NF-κB essential modulator) is a bridging adaptor indispensable for viral activation of interferon (IFN) antiviral response. Herein, we show that hepatitis A virus (HAV) 3C protease (3C <jats:sup>pro</jats:sup> ) cleaves NEMO at the Q304 residue, negating its signaling adaptor function and abrogating viral induction of IFN-β synthesis via the retinoic acid-inducible gene I/melanoma differentiation-associated protein 5 (RIG-I/MDA5) and Toll-like receptor 3 (TLR3) pathways. NEMO cleavage and IFN antagonism, however, were lost upon ablation of the catalytic activity of 3C <jats:sup>pro</jats:sup> . These data describe a novel immune evasion mechanism of HAV. </jats:p> Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon Journal of Virology
doi_str_mv 10.1128/jvi.00869-14
facet_avail Online
Free
finc_class_facet Medizin
Biologie
format ElectronicArticle
fullrecord blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qdmkuMDA4NjktMTQ
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qdmkuMDA4NjktMTQ
institution DE-Gla1
DE-Zi4
DE-15
DE-Pl11
DE-Rs1
DE-105
DE-14
DE-Ch1
DE-L229
DE-D275
DE-Bn3
DE-Brt1
DE-Zwi2
DE-D161
imprint American Society for Microbiology, 2014
imprint_str_mv American Society for Microbiology, 2014
issn 0022-538X
1098-5514
issn_str_mv 0022-538X
1098-5514
language English
mega_collection American Society for Microbiology (CrossRef)
match_str wang2014hepatitisavirus3cproteasecleavesnemotoimpairinductionofbetainterferon
publishDateSort 2014
publisher American Society for Microbiology
recordtype ai
record_format ai
series Journal of Virology
source_id 49
title Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_unstemmed Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_full Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_fullStr Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_full_unstemmed Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_short Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_sort hepatitis a virus 3c protease cleaves nemo to impair induction of beta interferon
topic Virology
Insect Science
Immunology
Microbiology
url http://dx.doi.org/10.1128/jvi.00869-14
publishDate 2014
physical 10252-10258
description <jats:title>ABSTRACT</jats:title> <jats:p> NEMO (NF-κB essential modulator) is a bridging adaptor indispensable for viral activation of interferon (IFN) antiviral response. Herein, we show that hepatitis A virus (HAV) 3C protease (3C <jats:sup>pro</jats:sup> ) cleaves NEMO at the Q304 residue, negating its signaling adaptor function and abrogating viral induction of IFN-β synthesis via the retinoic acid-inducible gene I/melanoma differentiation-associated protein 5 (RIG-I/MDA5) and Toll-like receptor 3 (TLR3) pathways. NEMO cleavage and IFN antagonism, however, were lost upon ablation of the catalytic activity of 3C <jats:sup>pro</jats:sup> . These data describe a novel immune evasion mechanism of HAV. </jats:p>
container_issue 17
container_start_page 10252
container_title Journal of Virology
container_volume 88
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
_version_ 1792346833195892739
geogr_code not assigned
last_indexed 2024-03-01T17:45:39.474Z
geogr_code_person not assigned
openURL url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Hepatitis+A+Virus+3C+Protease+Cleaves+NEMO+To+Impair+Induction+of+Beta+Interferon&rft.date=2014-09-01&genre=article&issn=1098-5514&volume=88&issue=17&spage=10252&epage=10258&pages=10252-10258&jtitle=Journal+of+Virology&atitle=Hepatitis+A+Virus+3C+Protease+Cleaves+NEMO+To+Impair+Induction+of+Beta+Interferon&aulast=Xiao&aufirst=Shaobo&rft_id=info%3Adoi%2F10.1128%2Fjvi.00869-14&rft.language%5B0%5D=eng
SOLR
_version_ 1792346833195892739
author Wang, Dang, Fang, Liurong, Wei, Dahai, Zhang, Huan, Luo, Rui, Chen, Huanchun, Li, Kui, Xiao, Shaobo
author_facet Wang, Dang, Fang, Liurong, Wei, Dahai, Zhang, Huan, Luo, Rui, Chen, Huanchun, Li, Kui, Xiao, Shaobo, Wang, Dang, Fang, Liurong, Wei, Dahai, Zhang, Huan, Luo, Rui, Chen, Huanchun, Li, Kui, Xiao, Shaobo
author_sort wang, dang
container_issue 17
container_start_page 10252
container_title Journal of Virology
container_volume 88
description <jats:title>ABSTRACT</jats:title> <jats:p> NEMO (NF-κB essential modulator) is a bridging adaptor indispensable for viral activation of interferon (IFN) antiviral response. Herein, we show that hepatitis A virus (HAV) 3C protease (3C <jats:sup>pro</jats:sup> ) cleaves NEMO at the Q304 residue, negating its signaling adaptor function and abrogating viral induction of IFN-β synthesis via the retinoic acid-inducible gene I/melanoma differentiation-associated protein 5 (RIG-I/MDA5) and Toll-like receptor 3 (TLR3) pathways. NEMO cleavage and IFN antagonism, however, were lost upon ablation of the catalytic activity of 3C <jats:sup>pro</jats:sup> . These data describe a novel immune evasion mechanism of HAV. </jats:p>
doi_str_mv 10.1128/jvi.00869-14
facet_avail Online, Free
finc_class_facet Medizin, Biologie
format ElectronicArticle
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
geogr_code not assigned
geogr_code_person not assigned
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qdmkuMDA4NjktMTQ
imprint American Society for Microbiology, 2014
imprint_str_mv American Society for Microbiology, 2014
institution DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161
issn 0022-538X, 1098-5514
issn_str_mv 0022-538X, 1098-5514
language English
last_indexed 2024-03-01T17:45:39.474Z
match_str wang2014hepatitisavirus3cproteasecleavesnemotoimpairinductionofbetainterferon
mega_collection American Society for Microbiology (CrossRef)
physical 10252-10258
publishDate 2014
publishDateSort 2014
publisher American Society for Microbiology
record_format ai
recordtype ai
series Journal of Virology
source_id 49
spelling Wang, Dang Fang, Liurong Wei, Dahai Zhang, Huan Luo, Rui Chen, Huanchun Li, Kui Xiao, Shaobo 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.00869-14 <jats:title>ABSTRACT</jats:title> <jats:p> NEMO (NF-κB essential modulator) is a bridging adaptor indispensable for viral activation of interferon (IFN) antiviral response. Herein, we show that hepatitis A virus (HAV) 3C protease (3C <jats:sup>pro</jats:sup> ) cleaves NEMO at the Q304 residue, negating its signaling adaptor function and abrogating viral induction of IFN-β synthesis via the retinoic acid-inducible gene I/melanoma differentiation-associated protein 5 (RIG-I/MDA5) and Toll-like receptor 3 (TLR3) pathways. NEMO cleavage and IFN antagonism, however, were lost upon ablation of the catalytic activity of 3C <jats:sup>pro</jats:sup> . These data describe a novel immune evasion mechanism of HAV. </jats:p> Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon Journal of Virology
spellingShingle Wang, Dang, Fang, Liurong, Wei, Dahai, Zhang, Huan, Luo, Rui, Chen, Huanchun, Li, Kui, Xiao, Shaobo, Journal of Virology, Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon, Virology, Insect Science, Immunology, Microbiology
title Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_full Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_fullStr Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_full_unstemmed Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_short Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
title_sort hepatitis a virus 3c protease cleaves nemo to impair induction of beta interferon
title_unstemmed Hepatitis A Virus 3C Protease Cleaves NEMO To Impair Induction of Beta Interferon
topic Virology, Insect Science, Immunology, Microbiology
url http://dx.doi.org/10.1128/jvi.00869-14