Hepatitis C virus exploits cyclophilin A to evade PKR

Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion...
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Autor*in:	Colpitts, Che C. [verfasserIn] Ridewood, Sophie [verfasserIn] Schneiderman, Bethany [verfasserIn] Warne, Justin [verfasserIn] Tabata, Keisuke [verfasserIn] Ng, Caitlin F. [verfasserIn] Bartenschlager, Ralf - 1958- [verfasserIn] Selwood, David L. [verfasserIn] Towers, Greg J. [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	June 16, 2020

Schlagwörter:	cyclosporine-a expression gene delivery inhibitors interferon isomerase activity ns5a protein-kinase replication rna-binding

Anmerkung:	Gesehen am 10.05.2021
Umfang:	25

Übergeordnetes Werk:	Enthalten in: eLife - Cambridge : eLife Sciences Publications, 2012, 9(2020) vom: Juni, Artikel-ID e52237, Seite 1-25
Übergeordnetes Werk:	volume:9 ; year:2020 ; month:06 ; elocationid:e52237 ; pages:1-25 ; extent:25

Links:	Volltext

DOI / URN:	10.7554/eLife.52237

Katalog-ID:	1757584331

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245	1	0	\|a Hepatitis C virus exploits cyclophilin A to evade PKR \|c Che C. Colpitts, Sophie Ridewood, Bethany Schneiderman, Justin Warne, Keisuke Tabata, Caitlin F. Ng, Ralf Bartenschlager, David L. Selwood, Greg J. Towers
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publishDate	2020
allfields	10.7554/eLife.52237 doi (DE-627)1757584331 (DE-599)KXP1757584331 (OCoLC)1341408879 DE-627 ger DE-627 rda eng Colpitts, Che C. verfasserin (DE-588)123323806X (DE-627)1757585494 aut Hepatitis C virus exploits cyclophilin A to evade PKR Che C. Colpitts, Sophie Ridewood, Bethany Schneiderman, Justin Warne, Keisuke Tabata, Caitlin F. Ng, Ralf Bartenschlager, David L. Selwood, Greg J. Towers June 16, 2020 25 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 10.05.2021 Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. Collectively, our study identifies a novel antiviral mechanism that harnesses cellular antiviral immunity to suppress viral replication. cyclosporine-a expression gene delivery inhibitors interferon isomerase activity ns5a protein-kinase replication rna-binding Ridewood, Sophie verfasserin aut Schneiderman, Bethany verfasserin aut Warne, Justin verfasserin aut Tabata, Keisuke verfasserin (DE-588)1156575842 (DE-627)1019382198 (DE-576)502273860 aut Ng, Caitlin F. verfasserin aut Bartenschlager, Ralf 1958- verfasserin (DE-588)1058097989 (DE-627)796390509 (DE-576)168706067 aut Selwood, David L. verfasserin aut Towers, Greg J. verfasserin aut Enthalten in eLife Cambridge : eLife Sciences Publications, 2012 9(2020) vom: Juni, Artikel-ID e52237, Seite 1-25 Online-Ressource (DE-627)728518384 (DE-600)2687154-3 (DE-576)372567576 2050-084X nnns volume:9 year:2020 month:06 elocationid:e52237 pages:1-25 extent:25 https://doi.org/10.7554/eLife.52237 Verlag Resolving-System Volltext GBV_USEFLAG_U GBV_ILN_21 ISIL_DE-46 SYSFLAG_1 GBV_KXP SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_2013 GBV_ILN_2013 ISIL_DE-16-250 AR 9 2020 6 e52237 1-25 25 21 01 0046 3969629683 xza 18-08-21 2013 01 DE-16-250 3927297097 00 --%%-- --%%-- --%%-- --%%-- l01 10-05-21 21 01 0046 https://doi.org/10.7554/eLife.52237 LF 2013 01 DE-16-250 00 s hd2020 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_25 2013 01 DE-16-250 04 p (DE-627)1572274212 Tabata, Keisuke 2013 01 DE-16-250 04 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1484102681 Bartenschlager, Ralf 2013 01 DE-16-250 05 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_7
spelling	10.7554/eLife.52237 doi (DE-627)1757584331 (DE-599)KXP1757584331 (OCoLC)1341408879 DE-627 ger DE-627 rda eng Colpitts, Che C. verfasserin (DE-588)123323806X (DE-627)1757585494 aut Hepatitis C virus exploits cyclophilin A to evade PKR Che C. Colpitts, Sophie Ridewood, Bethany Schneiderman, Justin Warne, Keisuke Tabata, Caitlin F. Ng, Ralf Bartenschlager, David L. Selwood, Greg J. Towers June 16, 2020 25 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 10.05.2021 Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. Collectively, our study identifies a novel antiviral mechanism that harnesses cellular antiviral immunity to suppress viral replication. cyclosporine-a expression gene delivery inhibitors interferon isomerase activity ns5a protein-kinase replication rna-binding Ridewood, Sophie verfasserin aut Schneiderman, Bethany verfasserin aut Warne, Justin verfasserin aut Tabata, Keisuke verfasserin (DE-588)1156575842 (DE-627)1019382198 (DE-576)502273860 aut Ng, Caitlin F. verfasserin aut Bartenschlager, Ralf 1958- verfasserin (DE-588)1058097989 (DE-627)796390509 (DE-576)168706067 aut Selwood, David L. verfasserin aut Towers, Greg J. verfasserin aut Enthalten in eLife Cambridge : eLife Sciences Publications, 2012 9(2020) vom: Juni, Artikel-ID e52237, Seite 1-25 Online-Ressource (DE-627)728518384 (DE-600)2687154-3 (DE-576)372567576 2050-084X nnns volume:9 year:2020 month:06 elocationid:e52237 pages:1-25 extent:25 https://doi.org/10.7554/eLife.52237 Verlag Resolving-System Volltext GBV_USEFLAG_U GBV_ILN_21 ISIL_DE-46 SYSFLAG_1 GBV_KXP SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_2013 GBV_ILN_2013 ISIL_DE-16-250 AR 9 2020 6 e52237 1-25 25 21 01 0046 3969629683 xza 18-08-21 2013 01 DE-16-250 3927297097 00 --%%-- --%%-- --%%-- --%%-- l01 10-05-21 21 01 0046 https://doi.org/10.7554/eLife.52237 LF 2013 01 DE-16-250 00 s hd2020 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_25 2013 01 DE-16-250 04 p (DE-627)1572274212 Tabata, Keisuke 2013 01 DE-16-250 04 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1484102681 Bartenschlager, Ralf 2013 01 DE-16-250 05 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_7
allfields_unstemmed	10.7554/eLife.52237 doi (DE-627)1757584331 (DE-599)KXP1757584331 (OCoLC)1341408879 DE-627 ger DE-627 rda eng Colpitts, Che C. verfasserin (DE-588)123323806X (DE-627)1757585494 aut Hepatitis C virus exploits cyclophilin A to evade PKR Che C. Colpitts, Sophie Ridewood, Bethany Schneiderman, Justin Warne, Keisuke Tabata, Caitlin F. Ng, Ralf Bartenschlager, David L. Selwood, Greg J. Towers June 16, 2020 25 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 10.05.2021 Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. Collectively, our study identifies a novel antiviral mechanism that harnesses cellular antiviral immunity to suppress viral replication. cyclosporine-a expression gene delivery inhibitors interferon isomerase activity ns5a protein-kinase replication rna-binding Ridewood, Sophie verfasserin aut Schneiderman, Bethany verfasserin aut Warne, Justin verfasserin aut Tabata, Keisuke verfasserin (DE-588)1156575842 (DE-627)1019382198 (DE-576)502273860 aut Ng, Caitlin F. verfasserin aut Bartenschlager, Ralf 1958- verfasserin (DE-588)1058097989 (DE-627)796390509 (DE-576)168706067 aut Selwood, David L. verfasserin aut Towers, Greg J. verfasserin aut Enthalten in eLife Cambridge : eLife Sciences Publications, 2012 9(2020) vom: Juni, Artikel-ID e52237, Seite 1-25 Online-Ressource (DE-627)728518384 (DE-600)2687154-3 (DE-576)372567576 2050-084X nnns volume:9 year:2020 month:06 elocationid:e52237 pages:1-25 extent:25 https://doi.org/10.7554/eLife.52237 Verlag Resolving-System Volltext GBV_USEFLAG_U GBV_ILN_21 ISIL_DE-46 SYSFLAG_1 GBV_KXP SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_2013 GBV_ILN_2013 ISIL_DE-16-250 AR 9 2020 6 e52237 1-25 25 21 01 0046 3969629683 xza 18-08-21 2013 01 DE-16-250 3927297097 00 --%%-- --%%-- --%%-- --%%-- l01 10-05-21 21 01 0046 https://doi.org/10.7554/eLife.52237 LF 2013 01 DE-16-250 00 s hd2020 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_25 2013 01 DE-16-250 04 p (DE-627)1572274212 Tabata, Keisuke 2013 01 DE-16-250 04 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1484102681 Bartenschlager, Ralf 2013 01 DE-16-250 05 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_7
allfieldsGer	10.7554/eLife.52237 doi (DE-627)1757584331 (DE-599)KXP1757584331 (OCoLC)1341408879 DE-627 ger DE-627 rda eng Colpitts, Che C. verfasserin (DE-588)123323806X (DE-627)1757585494 aut Hepatitis C virus exploits cyclophilin A to evade PKR Che C. Colpitts, Sophie Ridewood, Bethany Schneiderman, Justin Warne, Keisuke Tabata, Caitlin F. Ng, Ralf Bartenschlager, David L. Selwood, Greg J. Towers June 16, 2020 25 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 10.05.2021 Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. Collectively, our study identifies a novel antiviral mechanism that harnesses cellular antiviral immunity to suppress viral replication. cyclosporine-a expression gene delivery inhibitors interferon isomerase activity ns5a protein-kinase replication rna-binding Ridewood, Sophie verfasserin aut Schneiderman, Bethany verfasserin aut Warne, Justin verfasserin aut Tabata, Keisuke verfasserin (DE-588)1156575842 (DE-627)1019382198 (DE-576)502273860 aut Ng, Caitlin F. verfasserin aut Bartenschlager, Ralf 1958- verfasserin (DE-588)1058097989 (DE-627)796390509 (DE-576)168706067 aut Selwood, David L. verfasserin aut Towers, Greg J. verfasserin aut Enthalten in eLife Cambridge : eLife Sciences Publications, 2012 9(2020) vom: Juni, Artikel-ID e52237, Seite 1-25 Online-Ressource (DE-627)728518384 (DE-600)2687154-3 (DE-576)372567576 2050-084X nnns volume:9 year:2020 month:06 elocationid:e52237 pages:1-25 extent:25 https://doi.org/10.7554/eLife.52237 Verlag Resolving-System Volltext GBV_USEFLAG_U GBV_ILN_21 ISIL_DE-46 SYSFLAG_1 GBV_KXP SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_2013 GBV_ILN_2013 ISIL_DE-16-250 AR 9 2020 6 e52237 1-25 25 21 01 0046 3969629683 xza 18-08-21 2013 01 DE-16-250 3927297097 00 --%%-- --%%-- --%%-- --%%-- l01 10-05-21 21 01 0046 https://doi.org/10.7554/eLife.52237 LF 2013 01 DE-16-250 00 s hd2020 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_25 2013 01 DE-16-250 04 p (DE-627)1572274212 Tabata, Keisuke 2013 01 DE-16-250 04 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1484102681 Bartenschlager, Ralf 2013 01 DE-16-250 05 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_7
allfieldsSound	10.7554/eLife.52237 doi (DE-627)1757584331 (DE-599)KXP1757584331 (OCoLC)1341408879 DE-627 ger DE-627 rda eng Colpitts, Che C. verfasserin (DE-588)123323806X (DE-627)1757585494 aut Hepatitis C virus exploits cyclophilin A to evade PKR Che C. Colpitts, Sophie Ridewood, Bethany Schneiderman, Justin Warne, Keisuke Tabata, Caitlin F. Ng, Ralf Bartenschlager, David L. Selwood, Greg J. Towers June 16, 2020 25 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 10.05.2021 Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. Collectively, our study identifies a novel antiviral mechanism that harnesses cellular antiviral immunity to suppress viral replication. cyclosporine-a expression gene delivery inhibitors interferon isomerase activity ns5a protein-kinase replication rna-binding Ridewood, Sophie verfasserin aut Schneiderman, Bethany verfasserin aut Warne, Justin verfasserin aut Tabata, Keisuke verfasserin (DE-588)1156575842 (DE-627)1019382198 (DE-576)502273860 aut Ng, Caitlin F. verfasserin aut Bartenschlager, Ralf 1958- verfasserin (DE-588)1058097989 (DE-627)796390509 (DE-576)168706067 aut Selwood, David L. verfasserin aut Towers, Greg J. verfasserin aut Enthalten in eLife Cambridge : eLife Sciences Publications, 2012 9(2020) vom: Juni, Artikel-ID e52237, Seite 1-25 Online-Ressource (DE-627)728518384 (DE-600)2687154-3 (DE-576)372567576 2050-084X nnns volume:9 year:2020 month:06 elocationid:e52237 pages:1-25 extent:25 https://doi.org/10.7554/eLife.52237 Verlag Resolving-System Volltext GBV_USEFLAG_U GBV_ILN_21 ISIL_DE-46 SYSFLAG_1 GBV_KXP SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_2013 GBV_ILN_2013 ISIL_DE-16-250 AR 9 2020 6 e52237 1-25 25 21 01 0046 3969629683 xza 18-08-21 2013 01 DE-16-250 3927297097 00 --%%-- --%%-- --%%-- --%%-- l01 10-05-21 21 01 0046 https://doi.org/10.7554/eLife.52237 LF 2013 01 DE-16-250 00 s hd2020 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_25 2013 01 DE-16-250 04 p (DE-627)1572274212 Tabata, Keisuke 2013 01 DE-16-250 04 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1484102681 Bartenschlager, Ralf 2013 01 DE-16-250 05 k (DE-627)1495544966 Zentrum für Infektiologie 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_7
language	English
source	Enthalten in eLife 9(2020) vom: Juni, Artikel-ID e52237, Seite 1-25 volume:9 year:2020 month:06 elocationid:e52237 pages:1-25 extent:25
sourceStr	Enthalten in eLife 9(2020) vom: Juni, Artikel-ID e52237, Seite 1-25 volume:9 year:2020 month:06 elocationid:e52237 pages:1-25 extent:25
format_phy_str_mv	Article
building	21:z 2013:0
institution	findex.gbv.de
selectbib_iln_str_mv	21@za 2013@01
topic_facet	cyclosporine-a expression gene delivery inhibitors interferon isomerase activity ns5a protein-kinase replication rna-binding
sw_local_iln_str_mv	2013:hd2020 DE-16-250:hd2020 2013:wissenschaftlicher Artikel (Zeitschrift) DE-16-250:wissenschaftlicher Artikel (Zeitschrift) 2013:per_9 DE-16-250:per_9 2013:s_25 DE-16-250:s_25 2013:Tabata, Keisuke DE-16-250:Tabata, Keisuke 2013:Zentrum für Infektiologie DE-16-250:Zentrum für Infektiologie 2013:Verfasser DE-16-250:Verfasser 2013:pos_5 DE-16-250:pos_5 2013:Bartenschlager, Ralf DE-16-250:Bartenschlager, Ralf 2013:pos_7 DE-16-250:pos_7
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container_title	eLife
authorswithroles_txt_mv	Colpitts, Che C. @@aut@@ Ridewood, Sophie @@aut@@ Schneiderman, Bethany @@aut@@ Warne, Justin @@aut@@ Tabata, Keisuke @@aut@@ Ng, Caitlin F. @@aut@@ Bartenschlager, Ralf @@aut@@ Selwood, David L. @@aut@@ Towers, Greg J. @@aut@@
publishDateDaySort_date	2020-06-01T00:00:00Z
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language_de	englisch
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title	Hepatitis C virus exploits cyclophilin A to evade PKR
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title_full	Hepatitis C virus exploits cyclophilin A to evade PKR Che C. Colpitts, Sophie Ridewood, Bethany Schneiderman, Justin Warne, Keisuke Tabata, Caitlin F. Ng, Ralf Bartenschlager, David L. Selwood, Greg J. Towers
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title_sort	hepatitis c virus exploits cyclophilin a to evade pkr
title_auth	Hepatitis C virus exploits cyclophilin A to evade PKR
abstract	Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. Collectively, our study identifies a novel antiviral mechanism that harnesses cellular antiviral immunity to suppress viral replication. Gesehen am 10.05.2021
abstractGer	Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. Collectively, our study identifies a novel antiviral mechanism that harnesses cellular antiviral immunity to suppress viral replication. Gesehen am 10.05.2021
abstract_unstemmed	Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. Collectively, our study identifies a novel antiviral mechanism that harnesses cellular antiviral immunity to suppress viral replication. Gesehen am 10.05.2021
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title_short	Hepatitis C virus exploits cyclophilin A to evade PKR
url	https://doi.org/10.7554/eLife.52237
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up_date	2024-07-04T19:06:33.900Z
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fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">1757584331</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230428185519.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">210510s2020 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.7554/eLife.52237</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)1757584331</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)KXP1757584331</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(OCoLC)1341408879</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Colpitts, Che C.</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(DE-588)123323806X</subfield><subfield code="0">(DE-627)1757585494</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Hepatitis C virus exploits cyclophilin A to evade PKR</subfield><subfield code="c">Che C. Colpitts, Sophie Ridewood, Bethany Schneiderman, Justin Warne, Keisuke Tabata, Caitlin F. Ng, Ralf Bartenschlager, David L. Selwood, Greg J. Towers</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">June 16, 2020</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">25</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">Gesehen am 10.05.2021</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Counteracting innate immunity is essential for successful viral replication. Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. Here, we show that hepatitis C virus (HCV) co-opts the host protein CypA to aid evasion of antiviral responses dependent on the effector protein kinase R (PKR). Pharmacological inhibition of CypA rescues PKR from antagonism by HCV NS5A, leading to activation of an interferon regulatory factor-1 (IRF1)-driven cell intrinsic antiviral program that inhibits viral replication. These findings further the understanding of the complexity of Cyp-virus interactions, provide mechanistic insight into the remarkably broad antiviral spectrum of Cyp inhibitors, and uncover novel aspects of PKR activity and regulation. 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Hepatitis C virus exploits cyclophilin A to evade PKR

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