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The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/ MDA5 activation.

Identifieur interne : 000B17 ( PubMed/Curation ); précédent : 000B16; suivant : 000B18

The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/ MDA5 activation.

Auteurs : Zhen Ding [République populaire de Chine] ; Liurong Fang [République populaire de Chine] ; Shuangling Yuan [République populaire de Chine] ; Ling Zhao [République populaire de Chine] ; Xunlei Wang [République populaire de Chine] ; Siwen Long [République populaire de Chine] ; Mohan Wang [République populaire de Chine] ; Dang Wang [République populaire de Chine] ; Mohamed Frahat Foda [République populaire de Chine] ; Shaobo Xiao [République populaire de Chine]

Source :

Oncotarget [ 1949-2553 ] ; 2017.

RBID : pubmed:28591694

Descripteurs français

KwdFr :
- ARN double brin (métabolisme), Animaux, Humains, Hélicase IFIH1 inductrice de l'interféron (métabolisme), Interféron bêta (biosynthèse), Interféron bêta (génétique), Interféron bêta (métabolisme), Liaison aux protéines, Lignée cellulaire, Protéine-58 à domaine DEAD (métabolisme), Protéines nucléocapside (métabolisme), Régions promotrices (génétique), Souris, Virus Sendai (physiologie), Virus de l'hépatite murine (physiologie), eIF-2 Kinase (métabolisme).
MESH :
- biosynthèse : Interféron bêta.
- génétique : Interféron bêta.
- métabolisme : ARN double brin, Hélicase IFIH1 inductrice de l'interféron, Interféron bêta, Protéine-58 à domaine DEAD, Protéines nucléocapside, eIF-2 Kinase.
- physiologie : Virus Sendai, Virus de l'hépatite murine.
- Animaux, Humains, Liaison aux protéines, Lignée cellulaire, Régions promotrices (génétique), Souris.

English descriptors

KwdEn :
- Animals, Cell Line, DEAD Box Protein 58 (metabolism), Humans, Interferon-Induced Helicase, IFIH1 (metabolism), Interferon-beta (biosynthesis), Interferon-beta (genetics), Interferon-beta (metabolism), Mice, Murine hepatitis virus (physiology), Nucleocapsid Proteins (metabolism), Promoter Regions, Genetic, Protein Binding, RNA, Double-Stranded (metabolism), Sendai virus (physiology), eIF-2 Kinase (metabolism).
MESH :
- chemical , biosynthesis : Interferon-beta.
- chemical , genetics : Interferon-beta.
- chemical , metabolism : DEAD Box Protein 58, Interferon-Induced Helicase, IFIH1, Interferon-beta, Nucleocapsid Proteins, RNA, Double-Stranded, eIF-2 Kinase.
- physiology : Murine hepatitis virus, Sendai virus.
- Animals, Cell Line, Humans, Mice, Promoter Regions, Genetic, Protein Binding.

Abstract

Coronaviruses (CoVs) are a huge threat to both humans and animals and have evolved elaborate mechanisms to antagonize interferons (IFNs). Nucleocapsid (N) protein is the most abundant viral protein in CoV-infected cells, and has been identified as an innate immunity antagonist in several CoVs, including mouse hepatitis virus (MHV) and severe acute respiratory syndrome (SARS)-CoV. However, the underlying molecular mechanism(s) remain unclear. In this study, we found that MHV N protein inhibited Sendai virus and poly(I:C)-induced IFN-β production by targeting a molecule upstream of retinoic acid-induced gene I (RIG-I) and melanoma differentiation gene 5 (MDA5). Further studies showed that both MHV and SARS-CoV N proteins directly interacted with protein activator of protein kinase R (PACT), a cellular dsRNA-binding protein that can bind to RIG-I and MDA5 to activate IFN production. The N-PACT interaction sequestered the association of PACT and RIG-I/MDA5, which in turn inhibited IFN-β production. However, the N proteins from porcine epidemic diarrhea virus (PEDV) and porcine reproductive and respiratory syndrome virus (PRRSV), which are also classified in the order Nidovirales, did not interact and counteract with PACT. Taken together, our present study confirms that both MHV and SARS-CoV N proteins can perturb the function of cellular PACT to circumvent the innate antiviral response. However, this strategy does not appear to be used by all CoVs N proteins.

DOI: 10.18632/oncotarget.17912
PubMed: 28591694

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<term>Interferon-Induced Helicase, IFIH1 (metabolism)</term>
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<term>Interferon-beta (genetics)</term>
<term>Interferon-beta (metabolism)</term>
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<term>Interféron bêta (biosynthèse)</term>
<term>Interféron bêta (génétique)</term>
<term>Interféron bêta (métabolisme)</term>
<term>Liaison aux protéines</term>
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<term>Nucleocapsid Proteins</term>
<term>RNA, Double-Stranded</term>
<term>eIF-2 Kinase</term>
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<front><div type="abstract" xml:lang="en">Coronaviruses (CoVs) are a huge threat to both humans and animals and have evolved elaborate mechanisms to antagonize interferons (IFNs). Nucleocapsid (N) protein is the most abundant viral protein in CoV-infected cells, and has been identified as an innate immunity antagonist in several CoVs, including mouse hepatitis virus (MHV) and severe acute respiratory syndrome (SARS)-CoV. However, the underlying molecular mechanism(s) remain unclear. In this study, we found that MHV N protein inhibited Sendai virus and poly(I:C)-induced IFN-β production by targeting a molecule upstream of retinoic acid-induced gene I (RIG-I) and melanoma differentiation gene 5 (MDA5). Further studies showed that both MHV and SARS-CoV N proteins directly interacted with protein activator of protein kinase R (PACT), a cellular dsRNA-binding protein that can bind to RIG-I and MDA5 to activate IFN production. The N-PACT interaction sequestered the association of PACT and RIG-I/MDA5, which in turn inhibited IFN-β production. However, the N proteins from porcine epidemic diarrhea virus (PEDV) and porcine reproductive and respiratory syndrome virus (PRRSV), which are also classified in the order Nidovirales, did not interact and counteract with PACT. Taken together, our present study confirms that both MHV and SARS-CoV N proteins can perturb the function of cellular PACT to circumvent the innate antiviral response. However, this strategy does not appear to be used by all CoVs N proteins.</div>
</front>
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<DateCompleted><Year>2018</Year>
<Month>04</Month>
<Day>23</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<JournalIssue CitedMedium="Internet"><Volume>8</Volume>
<Issue>30</Issue>
<PubDate><Year>2017</Year>
<Month>Jul</Month>
<Day>25</Day>
</PubDate>
</JournalIssue>
<Title>Oncotarget</Title>
<ISOAbbreviation>Oncotarget</ISOAbbreviation>
</Journal>
<ArticleTitle>The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/ MDA5 activation.</ArticleTitle>
<Pagination><MedlinePgn>49655-49670</MedlinePgn>
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<ELocationID EIdType="doi" ValidYN="Y">10.18632/oncotarget.17912</ELocationID>
<Abstract><AbstractText>Coronaviruses (CoVs) are a huge threat to both humans and animals and have evolved elaborate mechanisms to antagonize interferons (IFNs). Nucleocapsid (N) protein is the most abundant viral protein in CoV-infected cells, and has been identified as an innate immunity antagonist in several CoVs, including mouse hepatitis virus (MHV) and severe acute respiratory syndrome (SARS)-CoV. However, the underlying molecular mechanism(s) remain unclear. In this study, we found that MHV N protein inhibited Sendai virus and poly(I:C)-induced IFN-β production by targeting a molecule upstream of retinoic acid-induced gene I (RIG-I) and melanoma differentiation gene 5 (MDA5). Further studies showed that both MHV and SARS-CoV N proteins directly interacted with protein activator of protein kinase R (PACT), a cellular dsRNA-binding protein that can bind to RIG-I and MDA5 to activate IFN production. The N-PACT interaction sequestered the association of PACT and RIG-I/MDA5, which in turn inhibited IFN-β production. However, the N proteins from porcine epidemic diarrhea virus (PEDV) and porcine reproductive and respiratory syndrome virus (PRRSV), which are also classified in the order Nidovirales, did not interact and counteract with PACT. Taken together, our present study confirms that both MHV and SARS-CoV N proteins can perturb the function of cellular PACT to circumvent the innate antiviral response. However, this strategy does not appear to be used by all CoVs N proteins.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ding</LastName>
<ForeName>Zhen</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Fang</LastName>
<ForeName>Liurong</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yuan</LastName>
<ForeName>Shuangling</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070, China.</Affiliation>
</AffiliationInfo>
</Author>
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   |texte=   The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/ MDA5 activation.
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The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/ MDA5 activation.

The nucleocapsid proteins of mouse hepatitis virus and severe acute respiratory syndrome coronavirus share the same IFN-β antagonizing mechanism: attenuation of PACT-mediated RIG-I/ MDA5 activation.

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