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10.1016/j.str.2022.05.020

http://scihub22266oqcxt.onion/10.1016/j.str.2022.05.020
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35716662!9212912!35716662
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suck abstract from ncbi


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pmid35716662      Structure 2022 ; 30 (9): 1224-1232.e5
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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.
  • |*COVID-19/virology[MESH]
  • |Cell Cycle Proteins/*metabolism[MESH]
  • |Coronavirus Envelope Proteins/*metabolism[MESH]
  • |Humans[MESH]
  • |Nuclear Proteins/metabolism[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |SARS-CoV-2/*physiology[MESH]


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