Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, Jiangsu, China.
Key Laboratory of Animal Diseases, Diagnostics, and Immunology, Ministry of Agriculture, Nanjing, Jiangsu, China.
BMC Vet Res. 2021 Jun 26;17(1):227. doi: 10.1186/s12917-021-02926-6.
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.
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.
Our data are likely to support the future investigation of the underlying mechanism of P1 infection and pathogenesis.
猪圆环病毒样病毒 P1 是一种相对较新的病毒，与断奶后多系统消耗综合征、先天性震颤和猪流产密切相关。P1 病毒感染和发病机制的分子机制尚不完全清楚。为了分析 P1 及其宿主的相互作用，我们使用酵母双杂交（Y2H）试验来鉴定与 P1 病毒 Cap 相互作用的细胞蛋白。在这项研究中，P1 病毒的 Cap 没有自我激活和毒性作用于酵母细胞，并被用作诱饵来筛选从胰腺组织制备的 Y2H 文库。
发现五个细胞蛋白（EEP、Ral GDS、Bcl-2-L-12、CPS1 和一个未鉴定的蛋白）与 P1 Cap 相互作用。Cap 和 Ral GDS 之间的相互作用通过共免疫沉淀得到证实。
我们的数据可能支持对 P1 感染和发病机制的潜在机制进行进一步研究。
