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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Bibliographic Details
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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Summary: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.
ISSN:1098-5514
DOI:10.1128/JVI.02807-12