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Poly(C)-binding protein 1, a novel N(pro)-interacting protein involved in classical swine fever virus growth

N(pro) is a multifunctional autoprotease unique to pestiviruses. The interacting partners of the N(pro) protein of classical swine fever virus (CSFV), a swine pestivirus, have been insufficiently defined. Using a yeast two-hybrid screen, we identified poly(C)-binding protein 1 (PCBP1) as a novel int...

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Published in:	Journal of virology 2013-02, Vol.87 (4), p.2072-2080
Main Authors:	Li, Dan, Li, Su, Sun, Yuan, Dong, Hong, Li, Yongfeng, Zhao, Bibo, Guo, Dongwei, Weng, Changjiang, Qiu, Hua-Ji
Format:	Article
Language:	English
Subjects:	Animals Cell Line Centrifugation Classical swine fever virus - growth & development Endopeptidases - metabolism Gene Knockdown Techniques Host-Pathogen Interactions Humans Immunoprecipitation Microscopy, Confocal Protein Binding Protein Interaction Mapping RNA, Small Interfering - metabolism RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Swine Two-Hybrid System Techniques Viral Proteins - metabolism
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container_end_page	2080
container_issue	4
container_start_page	2072
container_title	Journal of virology
container_volume	87
creator	Li, Dan Li, Su Sun, Yuan Dong, Hong Li, Yongfeng Zhao, Bibo Guo, Dongwei Weng, Changjiang Qiu, Hua-Ji
description	N(pro) is a multifunctional autoprotease unique to pestiviruses. The interacting partners of the N(pro) protein of classical swine fever virus (CSFV), a swine pestivirus, have been insufficiently defined. Using a yeast two-hybrid screen, we identified poly(C)-binding protein 1 (PCBP1) as a novel interacting partner of the CSFV N(pro) protein and confirmed this by coimmunoprecipitation, glutathione S-transferase (GST) pulldown, and confocal assays. Knockdown of PCBP1 by small interfering RNA suppressed CSFV growth, while overexpression of PCBP1 promoted CSFV growth. Furthermore, we showed that type I interferon was downregulated by PCBP1, as well as N(pro). Our results suggest that cellular PCBP1 positively modulates CSFV growth.
doi_str_mv	10.1128/JVI.02807-12
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The interacting partners of the N(pro) protein of classical swine fever virus (CSFV), a swine pestivirus, have been insufficiently defined. Using a yeast two-hybrid screen, we identified poly(C)-binding protein 1 (PCBP1) as a novel interacting partner of the CSFV N(pro) protein and confirmed this by coimmunoprecipitation, glutathione S-transferase (GST) pulldown, and confocal assays. Knockdown of PCBP1 by small interfering RNA suppressed CSFV growth, while overexpression of PCBP1 promoted CSFV growth. Furthermore, we showed that type I interferon was downregulated by PCBP1, as well as N(pro). 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The interacting partners of the N(pro) protein of classical swine fever virus (CSFV), a swine pestivirus, have been insufficiently defined. Using a yeast two-hybrid screen, we identified poly(C)-binding protein 1 (PCBP1) as a novel interacting partner of the CSFV N(pro) protein and confirmed this by coimmunoprecipitation, glutathione S-transferase (GST) pulldown, and confocal assays. Knockdown of PCBP1 by small interfering RNA suppressed CSFV growth, while overexpression of PCBP1 promoted CSFV growth. Furthermore, we showed that type I interferon was downregulated by PCBP1, as well as N(pro). 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source	PubMed Central Free; American Society for Microbiology Journals
subjects	Animals Cell Line Centrifugation Classical swine fever virus - growth & development Endopeptidases - metabolism Gene Knockdown Techniques Host-Pathogen Interactions Humans Immunoprecipitation Microscopy, Confocal Protein Binding Protein Interaction Mapping RNA, Small Interfering - metabolism RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Swine Two-Hybrid System Techniques Viral Proteins - metabolism
title	Poly(C)-binding protein 1, a novel N(pro)-interacting protein involved in classical swine fever virus growth
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