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The Structure of the Porcine Deltacoronavirus Main Protease Reveals a Conserved Target for the Design of Antivirals | |
2022-03 | |
Source Publication | VIRUSES-BASEL
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EISSN | 1999-4915 |
Volume | 14Issue:3 |
Status | 已发表 |
DOI | 10.3390/v14030486 |
Abstract | The existing zoonotic coronaviruses (CoVs) and viral genetic variants are important microbiological pathogens that cause severe disease in humans and animals. Currently, no effective broad-spectrum antiviral drugs against existing and emerging CoVs are available. The CoV main protease (M-pro) plays an essential role in viral replication, making it an ideal target for drug development. However, the structure of the Deltacoronavirus M-pro is still unavailable. Porcine deltacoronavirus (PDCoV) is a novel CoV that belongs to the genus Deltacoronavirus and causes atrophic enteritis, severe diarrhea, vomiting and dehydration in pigs. Here, we determined the structure of PDCoV M-pro complexed with a Michael acceptor inhibitor. Structural comparison showed that the backbone of PDCoV M-pro is similar to those of alpha-, beta- and gamma-CoV M(pro)s. The substrate-binding pocket of M-pro is well conserved in the subfamily Coronavirinae. In addition, we also observed that M(pro)s from the same genus adopted a similar conformation. Furthermore, the structure of PDCoV M-pro in complex with a Michael acceptor inhibitor revealed the mechanism of its inhibition of PDCoV M-pro. Our results provide a basis for the development of broad-spectrum antivirals against PDCoV and other CoVs. |
Keyword | coronaviruses porcine deltacoronavirus main protease broad-spectrum antivirals |
URL | 查看原文 |
Indexed By | SCI ; SCIE |
Language | 英语 |
Funding Project | Lingang Laboratory[LG202101-01-07] ; National Key R&D Program of China[2020YFA0707502] ; Science and Technology Commission of Shanghai Municipality["YDZX20213100001556","20XD1422900"] ; National Natural Science Foundation of China[92169109] |
WOS Research Area | Virology |
WOS Subject | Virology |
WOS ID | WOS:000774646800001 |
Publisher | MDPI |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/171475 |
Collection | 生命科学与技术学院 免疫化学研究所_PI研究组_杨海涛组 |
Corresponding Author | Zhang, Lei; Yang, Haitao |
Affiliation | 1.Tianjin Univ, Sch Life Sci, Tianjin 300072, Peoples R China 2.Tianjin Int Joint Acad Biotechnol & Med, Tianjin 300457, Peoples R China 3.Tianjin Univ Sci & Technol, Coll Biotechnol, Key Lab Ind Fermentat Microbiol, Tianjin Key Lab Ind Microbiol,Minist Educ, Tianjin 300457, Peoples R China 4.Shanghai Tech Univ, Shanghai Inst Adv Immunochem Studies, Shanghai 201210, Peoples R China 5.Shanghai Tech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China |
Corresponding Author Affilication | Shanghai Institute for Advanced Immunochemical Studies; School of Life Science and Technology |
Recommended Citation GB/T 7714 | Wang, Fenghua,Chen, Cheng,Wang, Zefang,et al. The Structure of the Porcine Deltacoronavirus Main Protease Reveals a Conserved Target for the Design of Antivirals[J]. VIRUSES-BASEL,2022,14(3). |
APA | Wang, Fenghua.,Chen, Cheng.,Wang, Zefang.,Han, Xu.,Shi, Peidian.,...&Yang, Haitao.(2022).The Structure of the Porcine Deltacoronavirus Main Protease Reveals a Conserved Target for the Design of Antivirals.VIRUSES-BASEL,14(3). |
MLA | Wang, Fenghua,et al."The Structure of the Porcine Deltacoronavirus Main Protease Reveals a Conserved Target for the Design of Antivirals".VIRUSES-BASEL 14.3(2022). |
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