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

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Zandian, Mohamad, Jang, Suk Min, Lachance, Catherine, Acharya, Arpan, Byrareddy, Siddappa N., Côté, Jacques, Kutateladze, Tatiana G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Protocol
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9613806/
https://www.ncbi.nlm.nih.gov/pubmed/36595918
http://dx.doi.org/10.1016/j.xpro.2022.101853
Descripción
Sumario: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)

Ejemplares similares