The Structure of the Porcine Deltacoronavirus Main Protease Reveals a Conserved Target for the Design of Antivirals
2022-03
Source PublicationVIRUSES-BASEL
EISSN1999-4915
Volume14Issue:3
Status已发表
DOI10.3390/v14030486
AbstractThe 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.
Keywordcoronaviruses porcine deltacoronavirus main protease broad-spectrum antivirals
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Indexed BySCI ; SCIE
Language英语
Funding ProjectLingang 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 AreaVirology
WOS SubjectVirology
WOS IDWOS:000774646800001
PublisherMDPI
Citation statistics
Cited Times:6[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttps://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 AuthorZhang, 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 AffilicationShanghai 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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