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Porcine teschovirus 2 induces an incomplete autophagic response in PK-15 cells.

Identifieur interne : 000523 ( Main/Exploration ); précédent : 000522; suivant : 000524

Porcine teschovirus 2 induces an incomplete autophagic response in PK-15 cells.

Auteurs : Yuanxing Gu [République populaire de Chine] ; Yingshan Zhou [République populaire de Chine] ; Xinfeng Shi [République populaire de Chine] ; Yongping Xin [République populaire de Chine] ; Ying Shan [République populaire de Chine] ; Cong Chen [République populaire de Chine] ; Tong Cao [République populaire de Chine] ; Weihuan Fang [République populaire de Chine] ; Xiaoliang Li [République populaire de Chine]

Source :

RBID : pubmed:29177545

Descripteurs français

English descriptors

Abstract

Autophagy is a homeostatic process that has been shown to be vital in the innate immune defense against pathogens. However, little is known about the regulatory role of autophagy in porcine teschovirus 2 (PTV-2) replication. In this study, we found that PTV-2 infection induces a strong increase in GFP-LC3 punctae and endogenous LC3 lipidation. However, PTV-2 infection did not enhance autophagic protein degradation. When cellular autophagy was pharmacologically inhibited by wortmannin or 3-methyladenine, PTV-2 replication increased. The increase in virus yield via autophagy inhibition was further confirmed by silencing atg5, which is required for autophagy. Furthermore, PTV-2 replication was suppressed when autophagy was activated by rapamycin. Together, the results suggest that PTV-2 infection activates incomplete autophagy and that autophagy then inhibits further PTV-2 replication.

DOI: 10.1007/s00705-017-3652-2
PubMed: 29177545


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Le document en format XML

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<term>Adenine (pharmacology)</term>
<term>Androstadienes (pharmacology)</term>
<term>Animals (MeSH)</term>
<term>Autophagy (drug effects)</term>
<term>Autophagy (genetics)</term>
<term>Autophagy-Related Protein 5 (antagonists & inhibitors)</term>
<term>Autophagy-Related Protein 5 (genetics)</term>
<term>Autophagy-Related Protein 5 (metabolism)</term>
<term>Cell Line (MeSH)</term>
<term>Epithelial Cells (drug effects)</term>
<term>Epithelial Cells (metabolism)</term>
<term>Epithelial Cells (virology)</term>
<term>Gene Expression Regulation (MeSH)</term>
<term>Genes, Reporter (MeSH)</term>
<term>Green Fluorescent Proteins (genetics)</term>
<term>Green Fluorescent Proteins (metabolism)</term>
<term>Host-Pathogen Interactions (MeSH)</term>
<term>Kidney (MeSH)</term>
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<term>Microtubule-Associated Proteins (metabolism)</term>
<term>RNA, Small Interfering (genetics)</term>
<term>RNA, Small Interfering (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
<term>Sirolimus (pharmacology)</term>
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<term>Teschovirus (drug effects)</term>
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<term>Cellules épithéliales (métabolisme)</term>
<term>Cellules épithéliales (virologie)</term>
<term>Gènes rapporteurs (MeSH)</term>
<term>Interactions hôte-pathogène (MeSH)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Petit ARN interférent (génétique)</term>
<term>Petit ARN interférent (métabolisme)</term>
<term>Protéine-5 associée à l'autophagie (antagonistes et inhibiteurs)</term>
<term>Protéine-5 associée à l'autophagie (génétique)</term>
<term>Protéine-5 associée à l'autophagie (métabolisme)</term>
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<term>Protéines associées aux microtubules (métabolisme)</term>
<term>Protéines à fluorescence verte (génétique)</term>
<term>Protéines à fluorescence verte (métabolisme)</term>
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<term>Régulation de l'expression des gènes (MeSH)</term>
<term>Réplication virale (effets des médicaments et des substances chimiques)</term>
<term>Réplication virale (génétique)</term>
<term>Sirolimus (pharmacologie)</term>
<term>Suidae (MeSH)</term>
<term>Teschovirus (croissance et développement)</term>
<term>Teschovirus (effets des médicaments et des substances chimiques)</term>
<term>Teschovirus (génétique)</term>
<term>Teschovirus (métabolisme)</term>
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<term>Teschovirus</term>
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<term>Teschovirus</term>
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<term>Protéine-5 associée à l'autophagie</term>
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<term>Protéines à fluorescence verte</term>
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<term>Teschovirus</term>
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<term>Teschovirus</term>
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<term>Genes, Reporter</term>
<term>Host-Pathogen Interactions</term>
<term>Kidney</term>
<term>Signal Transduction</term>
<term>Swine</term>
<term>Wortmannin</term>
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<term>Animaux</term>
<term>Gènes rapporteurs</term>
<term>Interactions hôte-pathogène</term>
<term>Lignée cellulaire</term>
<term>Rein</term>
<term>Régulation de l'expression des gènes</term>
<term>Suidae</term>
<term>Transduction du signal</term>
<term>Wortmannine</term>
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<div type="abstract" xml:lang="en">Autophagy is a homeostatic process that has been shown to be vital in the innate immune defense against pathogens. However, little is known about the regulatory role of autophagy in porcine teschovirus 2 (PTV-2) replication. In this study, we found that PTV-2 infection induces a strong increase in GFP-LC3 punctae and endogenous LC3 lipidation. However, PTV-2 infection did not enhance autophagic protein degradation. When cellular autophagy was pharmacologically inhibited by wortmannin or 3-methyladenine, PTV-2 replication increased. The increase in virus yield via autophagy inhibition was further confirmed by silencing atg5, which is required for autophagy. Furthermore, PTV-2 replication was suppressed when autophagy was activated by rapamycin. Together, the results suggest that PTV-2 infection activates incomplete autophagy and that autophagy then inhibits further PTV-2 replication.</div>
</front>
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<Year>2018</Year>
<Month>02</Month>
<Day>20</Day>
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<Year>2018</Year>
<Month>12</Month>
<Day>02</Day>
</DateRevised>
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<ISSN IssnType="Electronic">1432-8798</ISSN>
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<Volume>163</Volume>
<Issue>3</Issue>
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<Year>2018</Year>
<Month>Mar</Month>
</PubDate>
</JournalIssue>
<Title>Archives of virology</Title>
<ISOAbbreviation>Arch Virol</ISOAbbreviation>
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<ArticleTitle>Porcine teschovirus 2 induces an incomplete autophagic response in PK-15 cells.</ArticleTitle>
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<AbstractText>Autophagy is a homeostatic process that has been shown to be vital in the innate immune defense against pathogens. However, little is known about the regulatory role of autophagy in porcine teschovirus 2 (PTV-2) replication. In this study, we found that PTV-2 infection induces a strong increase in GFP-LC3 punctae and endogenous LC3 lipidation. However, PTV-2 infection did not enhance autophagic protein degradation. When cellular autophagy was pharmacologically inhibited by wortmannin or 3-methyladenine, PTV-2 replication increased. The increase in virus yield via autophagy inhibition was further confirmed by silencing atg5, which is required for autophagy. Furthermore, PTV-2 replication was suppressed when autophagy was activated by rapamycin. Together, the results suggest that PTV-2 infection activates incomplete autophagy and that autophagy then inhibits further PTV-2 replication.</AbstractText>
</Abstract>
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<Author ValidYN="Y">
<LastName>Gu</LastName>
<ForeName>Yuanxing</ForeName>
<Initials>Y</Initials>
<AffiliationInfo>
<Affiliation>Institute of Preventive Veterinary Medicine, Zhejiang University, Hangzhou, 310058, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Qingdao Agricultural University, Qingdao, 266109, China.</Affiliation>
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<AffiliationInfo>
<Affiliation>College of Animal Science and Technology, China-Australia Joint-Laboratory for Animal Health Big Data Analytics, Zhejiang Provincial Engineering Laboratory for Animal Health Inspection and Internet Technology, Zhejiang A&F University, Lin'an, 311300, China.</Affiliation>
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<Grant>
<GrantID>2015C02044</GrantID>
<Agency>Department of S&T of Zhejiang Province</Agency>
<Country></Country>
</Grant>
<Grant>
<GrantID>Y201635576</GrantID>
<Agency>Department of Education of Zhejiang Province</Agency>
<Country></Country>
</Grant>
<Grant>
<GrantID>2017ZDNT004</GrantID>
<Agency>Dabei Agricultural Discipline Development and Talent Training Fund</Agency>
<Country></Country>
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<ArticleDate DateType="Electronic">
<Year>2017</Year>
<Month>11</Month>
<Day>25</Day>
</ArticleDate>
</Article>
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<Country>Austria</Country>
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