Ubiquitin-Modified Proteome of SARS-CoV-2-Infected Host Cells Reveals Insights into Virus–Host Interaction and Pathogenesis

• DOI: 10.1021/acs.jproteome.0c00758
• Publication Date: 2021-03-05T12:48:59Z
• Authors: Huan Zhang; Huanying Zheng; Jinying Zhu; Qiao Dong; Jin Wang; Huahao Fan; Yangzhen Chen; Xi Zhang; Xiaohu Han; Qianlin Li; Jiahai Lu; Yigang Tong; Zeliang Chen
• Keywords: Proteome; Viral Pathogenesis; Pathogenesis; Coronavirus; Vero cell

The outbreak of coronavirus disease 2019 (COVID-19), which is caused by severe acute respiratory syndrome 2 (SARS-CoV-2), has posed a serious threat to global public health. mechanism pathogenesis and the host immune response SARS-CoV-2 infection are largely unknown. In present study, we applied quantitative proteomic technology identify quantify ubiquitination changes that occur in both virus Vero E6 cells during infection. By applying label-free, liquid chromatography with tandem mass spectrometry proteomics, 8943 lysine sites on 3086 proteins were identified, 138 104 quantified as significantly upregulated, while 828 447 downregulated at 72 h post-infection. Bioinformatics analysis suggested might modulate responses through important proteins, including USP5, IQGAP1, TRIM28, Hsp90. Ubiquitination modification was also observed 11 SAR-CoV-2 involved replication inhibition innate response. Our study provides new insights into interaction between well potential targets for prevention treatment COVID-19.