Characterization of multiple interactions between the envelope E protein of SARS-CoV-2 and human BRD4

Mohamad Zandian; Suk Min Jang; Catherine Lachance; Arpan Acharya; Siddappa N. Byrareddy; Jacques Côté; Tatiana G. Kutateladze

doi:10.1016/j.xpro.2022.101853

Characterization of multiple interactions between the envelope E protein of SARS-CoV-2 and human BRD4

Mohamad Zandian, Suk Min Jang, Catherine Lachance, Arpan Acharya, Siddappa N. Byrareddy, Jacques Côté, Tatiana G. Kutateladze

Research output: Contribution to journal › Article › peer-review

Abstract

The SARS-CoV-2 envelope (E) protein hijacks human BRD4 (bromodomain and extra-terminal domain protein 4). Here, we describe a protocol to characterize the interaction of the acetylated E protein with BRD4 in vivo. We detail steps to use NMR spectroscopy to map the binding interface and include steps to monitor the effect of BRD4 inhibitors in SARS-CoV-2-infected human lung bronchial epithelial cells. This approach could be applied to study interactions involving other viral and human proteins. For complete details on the use and execution of this protocol, please refer to Vann et al. (2022).¹

Original language	English (US)
Article number	101853
Journal	STAR Protocols
Volume	3
Issue number	4
DOIs	https://doi.org/10.1016/j.xpro.2022.101853
State	Published - Dec 16 2022

Keywords

Cell Biology
Microbiology
Molecular Biology
NMR
Protein Biochemistry
Structural Biology

ASJC Scopus subject areas

Neuroscience(all)
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)

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10.1016/j.xpro.2022.101853

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title = "Characterization of multiple interactions between the envelope E protein of SARS-CoV-2 and human BRD4",

abstract = "The SARS-CoV-2 envelope (E) protein hijacks human BRD4 (bromodomain and extra-terminal domain protein 4). Here, we describe a protocol to characterize the interaction of the acetylated E protein with BRD4 in vivo. We detail steps to use NMR spectroscopy to map the binding interface and include steps to monitor the effect of BRD4 inhibitors in SARS-CoV-2-infected human lung bronchial epithelial cells. This approach could be applied to study interactions involving other viral and human proteins. For complete details on the use and execution of this protocol, please refer to Vann et al. (2022).1",

keywords = "Cell Biology, Microbiology, Molecular Biology, NMR, Protein Biochemistry, Structural Biology",

author = "Mohamad Zandian and Jang, {Suk Min} and Catherine Lachance and Arpan Acharya and Byrareddy, {Siddappa N.} and Jacques C{\^o}t{\'e} and Kutateladze, {Tatiana G.}",

note = "Funding Information: This work was supported in part by grants from the NIH HL151334 , CA252707 , GM125195 , GM135671 , and AG067664 to T.G.K. and AI129745 and DA052845 to S.N.B. and a foundation grant from the CIHR to J.C. ( FDN-143314 ). Publisher Copyright: {\textcopyright} 2022 The Author(s)",

year = "2022",

month = dec,

day = "16",

doi = "10.1016/j.xpro.2022.101853",

language = "English (US)",

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AU - Zandian, Mohamad

AU - Jang, Suk Min

AU - Lachance, Catherine

AU - Acharya, Arpan

AU - Byrareddy, Siddappa N.

AU - Côté, Jacques

AU - Kutateladze, Tatiana G.

N1 - Funding Information: This work was supported in part by grants from the NIH HL151334 , CA252707 , GM125195 , GM135671 , and AG067664 to T.G.K. and AI129745 and DA052845 to S.N.B. and a foundation grant from the CIHR to J.C. ( FDN-143314 ). Publisher Copyright: © 2022 The Author(s)

PY - 2022/12/16

Y1 - 2022/12/16

N2 - The SARS-CoV-2 envelope (E) protein hijacks human BRD4 (bromodomain and extra-terminal domain protein 4). Here, we describe a protocol to characterize the interaction of the acetylated E protein with BRD4 in vivo. We detail steps to use NMR spectroscopy to map the binding interface and include steps to monitor the effect of BRD4 inhibitors in SARS-CoV-2-infected human lung bronchial epithelial cells. This approach could be applied to study interactions involving other viral and human proteins. For complete details on the use and execution of this protocol, please refer to Vann et al. (2022).1

AB - The SARS-CoV-2 envelope (E) protein hijacks human BRD4 (bromodomain and extra-terminal domain protein 4). Here, we describe a protocol to characterize the interaction of the acetylated E protein with BRD4 in vivo. We detail steps to use NMR spectroscopy to map the binding interface and include steps to monitor the effect of BRD4 inhibitors in SARS-CoV-2-infected human lung bronchial epithelial cells. This approach could be applied to study interactions involving other viral and human proteins. For complete details on the use and execution of this protocol, please refer to Vann et al. (2022).1

KW - Cell Biology

KW - Microbiology

KW - Molecular Biology

KW - NMR

KW - Protein Biochemistry

KW - Structural Biology

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AN - SCOPUS:85142287011

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JO - STAR Protocols

JF - STAR Protocols

SN - 2666-1667

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ER -

Characterization of multiple interactions between the envelope E protein of SARS-CoV-2 and human BRD4

Abstract

Keywords

ASJC Scopus subject areas

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