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Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Structure 2022 ; 30 (9): 1224-1232.e5 Nephropedia Template TP
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Binding of the SARS-CoV-2 envelope E protein to human BRD4 is essential for infection #MMPMID35716662
Vann KR; Acharya A; Jang SM; Lachance C; Zandian M; Holt TA; Smith AL; Pandey K; Durden DL; El-Gamal D; Cote J; Byrareddy SN; Kutateladze TG
Structure 2022[Sep]; 30 (9): 1224-1232.e5 PMID35716662show ga
Emerging new variants of SARS-CoV-2 and inevitable acquired drug resistance call for the continued search of new pharmacological targets to fight the potentially fatal infection. Here, we describe the mechanisms by which the E protein of SARS-CoV-2 hijacks the human transcriptional regulator BRD4. We found that SARS-CoV-2 E is acetylated in vivo and co-immunoprecipitates with BRD4 in human cells. Bromodomains (BDs) of BRD4 bind to the C-terminus of the E protein, acetylated by human acetyltransferase p300, whereas the ET domain of BRD4 recognizes the unmodified motif of the E protein. Inhibitors of BRD4 BDs, JQ1 or OTX015, decrease SARS-CoV-2 infectivity in lung bronchial epithelial cells, indicating that the acetyllysine binding function of BDs is necessary for the virus fitness and that BRD4 represents a potential anti-COVID-19 target. Our findings provide insight into molecular mechanisms that contribute to SARS-CoV-2 pathogenesis and shed light on a new strategy to block SARS-CoV-2 infection.