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FKBP8 interact with classical swine fever virus NS5A protein and promote virus RNA replication

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Abstract

The non-structural 5A (NS5A) protein of classical swine fever virus (CSFV) is proven to be involved in viral replication and can also modulate cellular signaling and host cellular responses via to its ability to interact with various cellular proteins. FKBP8 is also reported to promote virus replication. Here, we show that NS5A specifically interacts with FKBP8 through coimmunoprecipitation and GST-pulldown studies. Additionally, confocal microscopy study showed that NS5A and FKBP8 colocalized in the cytoplasm. Overexpression of FKBP8 via the eukaryotic expression plasmid pDsRED N1 significantly promoted viral RNA synthesis. The cells knockdown of FKBP8 by lentivirus-mediated shRNA markedly decreased the virus replication when infected with CSFV. These data suggest that FKBP8 plays a critical role in the viral life cycle, particularly during the virus RNA replication period. The investigation of FKBP8 protein functions may be beneficial for developing new strategies to treat CSFV infection.

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Acknowledgments

The research was supported by China National Science Funds (No. 31172339).

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Correspondence to Yanming Zhang.

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Author contributions

Helin Li and Cheng-cheng Zhang took part in all the experiments and wrote the manuscript. Yan-ming Zhang and Cheng-cheng Zhang designed the experiments. Kangkang Guo was charge of the plasmid construction and transfection. Fang Wang participated in Western blotting and CO-IP. Tianyue Zhao and Wulong Liang participated in cell culture and confocal microscopy. Qizhuang Lv made a contribution to the data analysis.

Conflict of interest

The authors declare that they have no conflict of interest.

Additional information

Edited by Juergen A Richt.

Helin li and Chengcheng Zhang have contributed equally to this work.

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Li, H., Zhang, C., Cui, H. et al. FKBP8 interact with classical swine fever virus NS5A protein and promote virus RNA replication. Virus Genes 52, 99–106 (2016). https://doi.org/10.1007/s11262-015-1286-6

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  • DOI: https://doi.org/10.1007/s11262-015-1286-6

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