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Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Proc+Natl+Acad+Sci+U+S+A 2022 ; 119 (30): e2123065119 Nephropedia Template TP
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The global succinylation of SARS-CoV-2-infected host cells reveals drug targets #MMPMID35858407
Liu Q; Wang H; Zhang H; Sui L; Li L; Xu W; Du S; Hao P; Jiang Y; Chen J; Qu X; Tian M; Zhao Y; Guo X; Wang X; Song W; Song G; Wei Z; Hou Z; Wang G; Sun M; Li X; Lu H; Zhuang X; Jin N; Zhao Y; Li C; Liao M
Proc Natl Acad Sci U S A 2022[Jul]; 119 (30): e2123065119 PMID35858407show ga
SARS-CoV-2, the causative agent of the COVID-19 pandemic, undergoes continuous evolution, highlighting an urgent need for development of novel antiviral therapies. Here we show a quantitative mass spectrometry-based succinylproteomics analysis of SARS-CoV-2 infection in Caco-2 cells, revealing dramatic reshape of succinylation on host and viral proteins. SARS-CoV-2 infection promotes succinylation of several key enzymes in the TCA, leading to inhibition of cellular metabolic pathways. We demonstrated that host protein succinylation is regulated by viral nonstructural protein (NSP14) through interaction with sirtuin 5 (SIRT5); overexpressed SIRT5 can effectively inhibit virus replication. We found succinylation inhibitors possess significant antiviral effects. We also found that SARS-CoV-2 nucleocapsid and membrane proteins underwent succinylation modification, which was conserved in SARS-CoV-2 and its variants. Collectively, our results uncover a regulatory mechanism of host protein posttranslational modification and cellular pathways mediated by SARS-CoV-2, which may become antiviral drug targets against COVID-19.