A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro

文献类型: 外文期刊

第一作者: Zhu, Xuejiao

作者: Zhu, Xuejiao;Fan, Baochao;Zhou, Junming;Wang, Dandan;Li, Bin;Zhu, Xuejiao;Fan, Baochao;Zhou, Junming;Wang, Dandan;Li, Bin;Zhu, Xuejiao;Fan, Baochao;Zhou, Junming;Wang, Dandan;Li, Bin;Fan, Baochao;Fan, Huiying;Li, Bin

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关键词: African swine fever virus; protein p22; GO KEGG pathways analysis; liquid chromatography; mass spectrometry

期刊名称:FRONTIERS IN VETERINARY SCIENCE ( 影响因子:3.412; 五年影响因子:3.588 )

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年卷期: 2021 年 8 卷

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收录情况: SCI

摘要: African swine fever virus (ASFV) has been identified as the agent of African swine fever, resulting in a mortality rate of nearly 100% in domestic pigs worldwide. Protein p22 encoded by gene KP177R has been reported to be localized at the inner envelope of the virus, while the function of p22 remains unclear. In this study, p22 interacting proteins of the host were identified by a high-throughput method and analyzed by Gene ontology terms and Kyoto Encyclopedia of Gene and Genomes (KEGG) pathways; numerous cellular proteins in 293-T that interacted with p22 protein were identified. These interacting proteins were related to the biological processes of binding, cell structure, signal transduction, cell adhesion, etc. At the same time, the interacted proteins participated in several KEGG pathways like ribosome, spliceosome, etc. The key proteins in the protein-protein interaction network were closely related to actin filament organization and movement, resulting in affecting the process of phagocytosis and endocytosis. A large number of proteins that interacted with p22 were identified, providing a large database, which should be very useful to elucidate the function of p22 in the near future, laying the foundation for elucidating the mechanism of ASFV.

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