期刊
CELL AND BIOSCIENCE
卷 11, 期 1, 页码 -出版社
BMC
DOI: 10.1186/s13578-021-00644-y
关键词
SARS-CoV-2; Interaction map; N; Nsp3; Replication
资金
- Natural Science Foundation of China [31971161, 31900546]
- Natural Science Foundation of Guangdong [2019A1515011332]
- Shenzhen Science and Technology Program [JCYJ20190807160615255, JCYJ20190807153203560]
The study identified multiple protein-protein interactions in SARS-CoV-2 viral proteins, with Nsp1 displaying the most interacting partners among all viral proteins. Specific interactions such as Nsp3.1/N, Nsp3.2/Nsp12, and Nsp10/Nsp14 were found to be bidirectional. Additionally, Nsp3.1 was shown to inhibit viral replication by interacting with N through its N-terminus.
Background Analysis of viral protein-protein interactions is an essential step to uncover the viral protein functions and the molecular mechanism for the assembly of a viral protein complex. We employed a mammalian two-hybrid system to screen all the viral proteins of SARS-CoV-2 for the protein-protein interactions. Results Our study detected 48 interactions, 14 of which were firstly reported here. Unlike Nsp1 of SARS-CoV, Nsp1 of SARS-CoV-2 has the most interacting partners among all the viral proteins and likely functions as a hub for the viral proteins. Five self-interactions were confirmed, and five interactions, Nsp1/Nsp3.1, Nsp3.1/N, Nsp3.2/Nsp12, Nsp10/Nsp14, and Nsp10/Nsp16, were determined to be positive bidirectionally. Using the replicon reporter system of SARS-CoV-2, we screened all viral Nsps for their impacts on the viral replication and revealed Nsp3.1, the N-terminus of Nsp3, significantly inhibited the replicon reporter gene expression. We found Nsp3 interacted with N through its acidic region at N-terminus, while N interacted with Nsp3 through its NTD, which is rich in the basic amino acids. Furthermore, using purified truncated N and Nsp3 proteins, we determined the direct interactions between Nsp3 and N protein. Conclusions Our findings provided a basis for understanding the functions of coronavirus proteins and supported the potential of interactions as the target for antiviral drug development.
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