A High Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus in Vitro
Abstract Background: African Swine Fever Virus (ASFV) has been identified as the agent of ASF, which has resulting in a mortality rate of nearly 100% in domestic pigs worldwide. Protein p22 encoded by pKP177L was reported to be localized at the inner envelope of the virus, while the function of p22 remains unclear.Methods: Protein p22 interacted proteins of the host were immune-precipitated and identified by Liquid Chromatography Mass Spectrometry, analyzed by Go terms and KEGG pathways. Results: Numerous cellular proteins in 293-T that interacted with p22 protein were identified. These interacted proteins were related to the biological processes of binding, cell structure, signal transduction, cell adhesion, etc., and their interactions. At the same time, the interacted proteins participated in several KEGG pathways like ribosome, splicesome, etc. The key proteins in PPI network were closely related to actin filament organization and movement, resulting in affecting the process of phagocytosis and endocytosis. Conclusions: The identified high number of proteins interacted with p22 and as a large database should be very useful to elucidate the function of p22 in the near future, and lay the foundation for elucidating the mechanism of ASFV.