蛋白酵素
蛋白质水解
Jurkat细胞
蛋白酶
生物
重组DNA
劈理(地质)
生物化学
病毒学
免疫系统
酶
遗传学
基因
T细胞
古生物学
断裂(地质)
作者
Shu Y. Luo,Eman Moussa,Joaquín López-Orozco,Alberto Felix-Lopez,Ray Ishida,Nawell Fayad,Erik Gomez‐Cardona,Henry Wang,Joyce A. Wilson,Anil Kumar,Tom C. Hobman,Olivier Julien
出处
期刊:ACS Infectious Diseases
[American Chemical Society]
日期:2023-04-03
卷期号:9 (4): 749-761
被引量:1
标识
DOI:10.1021/acsinfecdis.2c00458
摘要
The recent emergence of SARS-CoV-2 in the human population has caused a global pandemic. The virus encodes two proteases, Mpro and PLpro, that are thought to play key roles in the suppression of host protein synthesis and immune response evasion during infection. To identify the specific host cell substrates of these proteases, active recombinant SARS-CoV-2 Mpro and PLpro were added to A549 and Jurkat human cell lysates, and subtiligase-mediated N-terminomics was used to capture and enrich protease substrate fragments. The precise location of each cleavage site was identified using mass spectrometry. Here, we report the identification of over 200 human host proteins that are potential substrates for SARS-CoV-2 Mpro and PLpro and provide a global mapping of proteolysis for these two viral proteases in vitro. Modulating proteolysis of these substrates will increase our understanding of SARS-CoV-2 pathobiology and COVID-19.
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