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Interaction of porcine circovirus-like virus P1 capsid protein with host proteins

文献类型： 外文期刊

作者： Wen, Libin 1 ; Zhu, Jiaping 1 ; Zhang, Fengxi 1 ; Xiao, Qi 1 ; Xie, Jianping 1 ; He, Kongwang 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Vet Med, Nanjing, Jiangsu, Peoples R China

2.Minist Agr, Diagnost & Immunol, Key Lab Anim Dis, Nanjing, Jiangsu, Peoples R China

3.Jiangsu Coinnovat Ctr Prevent & Control, Control Important Anim Infect Dis & Zoonoses, Yangzhou, Jiangsu, Peoples R China

关键词： Porcine circovirus-like virus P1; yeast two-hybrid assay; Cap; cellular protein; co-immunoprecipitation

期刊名称：BMC VETERINARY RESEARCH （ 影响因子：2.741； 五年影响因子：2.955 ）

ISSN：

年卷期： 2021 年 17 卷 1 期

页码：

收录情况： SCI

摘要： Background Porcine circovirus-like virus P1 is a relatively new kind of virus that is closely related to the post-weaning multisystemic wasting syndrome, congenital tremors, and abortions in swine. The molecular mechanisms of P1 virus infection and pathogenesis are fully unknown. To analyze P1 and its host interactions, we used a yeast two-hybrid (Y2H) assay to identify cellular proteins interacting with the Cap of the P1 virus. In this study, the Cap of the P1 virus exhibited no self-activation and toxicity to yeast cells and was used as bait to screen the Y2H library prepared from the pancreas tissue. Results Five cellular proteins (EEP, Ral GDS, Bcl-2-L-12, CPS1, and one not identified) were found to interact with P1 Cap. The interaction between Cap and Ral GDS was confirmed by co-immunoprecipitation. Conclusions Our data are likely to support the future investigation of the underlying mechanism of P1 infection and pathogenesis.

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