Article(id=1238813312654299470, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1238813307784712441, articleNumber=null, orderNo=null, doi=10.13343/j.cnki.wsxb.20250733, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=research-article, receivedDate=1758902400000, receivedDateStr=2025-09-27, revisedDate=null, revisedDateStr=null, acceptedDate=1761580800000, acceptedDateStr=2025-10-28, onlineDate=1773285709775, onlineDateStr=2026-03-12, pubDate=1772553600000, pubDateStr=2026-03-04, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1773285709775, onlineIssueDateStr=2026-03-12, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1773285709775, creator=13701087609, updateTime=1773285709775, updator=13701087609, issue=Issue{id=1238813307784712441, tenantId=1146029695717560320, journalId=1192105938417971205, year='2026', volume='66', issue='3', pageStart='961', pageEnd='1466', issueExtLink='null', onlineDate='null', pubDate='null', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=null, createTime=1773285708614, creator=13701087609, updateTime=1773291912509, updator=13701087609, preIssue=null, nextIssue=null, ext={EN=IssueExt(id=1238839328915378858, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1238813307784712441, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1238839328915378859, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1238813307784712441, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null}, startPage=1007, endPage=1025, ext={EN=ArticleExt(id=1238813313103090034, articleId=1238813312654299470, tenantId=1146029695717560320, journalId=1192105938417971205, language=EN, title=Advances in coronavirus main protease functions and inhibitor screening methods, columnId=1192149543727808575, journalTitle=Acta Microbiologica Sinica, columnName=Review, runingTitle=null, highlight=null, articleAbstract=

Coronaviruses pose a serious threat to human and animal health. Their main protease (Mpro) plays a critical role in both the viral life cycle and host immune regulation, serving as a key target for the development of broad-spectrum anti-coronavirus drugs. The core function of Mpro lies in its specific cleavage of viral polyproteins pp1a and pp1ab to release functional non-structural proteins (NSPs), thereby driving the assembly of the viral replication/transcription complex. Additionally, Mpro can target and cleave key molecules in host immune signaling pathways, facilitating viral immune evasion. Given its dual roles and highly conserved catalytic center, the research on Mpro has become a major focus in the field. This review systematically outlines the structural features and functional diversity of Mpro, with an emphasis on its catalytic mechanism in the viral replication cycle and its role in mediating immune suppression. Furthermore, this article details the screening methods and design strategies for Mpro inhibitors, aiming to offer theoretical foundations and novel insights for the development of anti-coronavirus drugs targeting this critical protein.

, correspAuthors=Yu’e WANG, authorNote=null, correspAuthorsNote=, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=null, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, authorCompany=null, fund=null, authors=null, authorsList=Moukang XIONG, Junhai ZHU, Yu’e WANG), CN=ArticleExt(id=1238813317138010695, articleId=1238813312654299470, tenantId=1146029695717560320, journalId=1192105938417971205, language=CN, title=冠状病毒主蛋白酶功能及抑制剂筛选方法研究进展, columnId=1192149543882997826, journalTitle=微生物学报, columnName=综述, runingTitle=null, highlight=null, articleAbstract=

冠状病毒是严重威胁人类与动物健康的病原体。主蛋白酶(main protease, Mpro)在病毒生命周期及宿主免疫调节中均发挥着重要作用，是开发广谱抗冠状病毒药物的关键靶点。Mpro的核心作用在于特异性切割病毒多聚蛋白pp1a和pp1ab，以释放功能性非结构蛋白(non-structural proteins, NSPs)，进而驱动病毒复制/转录复合体的组装。此外，Mpro能够靶向切割宿主免疫信号通路中的关键分子，有利于病毒实现免疫逃逸。鉴于其功能的双重性以及催化中心的高度保守性，针对Mpro的研究已成为该领域的热点。本文系统概述了Mpro的结构特征与功能多样性，重点论述了其在病毒复制周期中的催化机制及介导免疫抑制的作用，进而详细探讨了Mpro抑制剂的筛选方法与设计策略，为针对该靶点的抗冠状病毒药物研发提供了理论依据和新思路。

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Nature Communications, 2021, 12: 3061., articleTitle=Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives, refAbstract=null)], funds=[Fund(id=1238891101097087483, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, awardId=CSTB2024NSCQ-MSX0467, language=EN, fundingSource=Natural Science Foundation of Chongqing(CSTB2024NSCQ-MSX0467), fundOrder=null, country=null), Fund(id=1238891101197750789, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, awardId=CSTB2024NSCQ-MSX0467, language=CN, fundingSource=重庆市自然科学基金(CSTB2024NSCQ-MSX0467), fundOrder=null, country=null), Fund(id=1238891101340357134, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, awardId=SWU-KR22036, language=EN, fundingSource=Fundamental Research Funds for the Central Universities(SWU-KR22036), fundOrder=null, country=null), Fund(id=1238891101457797657, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, awardId=SWU-KR22036, language=CN, fundingSource=中央高校基本科研业务费专项资金(SWU-KR22036), fundOrder=null, country=null)], companyList=[AuthorCompany(id=1238891095065677989, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, xref=null, ext=[AuthorCompanyExt(id=1238891095069872294, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, companyId=1238891095065677989, language=EN, country=null, province=null, city=null, postcode=null, companyName=null, departmentName=null, remark=College of Veterinary Medicine, Southwest University, Chongqing, China), AuthorCompanyExt(id=1238891095082455208, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, companyId=1238891095065677989, language=CN, country=null, province=null, city=null, postcode=null, companyName=null, departmentName=null, remark=西南大学 动物医学院，重庆)])], figs=[ArticleFig(id=1238891097116692765, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=EN, label=Figure 1, caption=The 3D structure of SARS-CoV-2 Mpro. Presented from two distinct perspectives, one monomer in the dimer is displayed in yellow, while the other monomer is shown in light blue and marked with an asterisk (*); PDB ID: 7EN8., figureFileSmall=4bBQKCy2GJ7OnqVJshKi/g==, figureFileBig=2+ciTxV4gYFVs5VeoEmqvw==, tableContent=null), ArticleFig(id=1238891097229938984, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=CN, label=图1, caption=SARS-CoV-2 Mpro三维结构。从2个不同视角呈现，二聚体中一个单体以黄色显示，另一个单体则以浅蓝显示并标注星号(*)；PDB ID: 7EN8。, figureFileSmall=4bBQKCy2GJ7OnqVJshKi/g==, figureFileBig=2+ciTxV4gYFVs5VeoEmqvw==, tableContent=null), ArticleFig(id=1238891097322213681, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=EN, label=Figure 2, caption=Hydrolysis mechanism of SARS-CoV-2 Mpro^[22]. Amino acids of the catalytic dyad and the substrate are depicted in blue and red, respectively. Created with BioGDP.com^[23]., figureFileSmall=s6SZPy/YQWm9CSGtygBZYw==, figureFileBig=y5On15eK2Pm249d4pkhRkg==, tableContent=null), ArticleFig(id=1238891097427071289, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=CN, label=图2, caption=冠状病毒Mpro的催化机制^[22]。催化二元组与底物氨基酸分别用蓝色和红色标示。, figureFileSmall=s6SZPy/YQWm9CSGtygBZYw==, figureFileBig=y5On15eK2Pm249d4pkhRkg==, tableContent=null), ArticleFig(id=1238891098882494788, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=EN, label=Figure 3, caption=The virtual screening for identifying Mpro inhibitors. ADMET: Absorption, distribution, metabolism, excretion, and toxicity. 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Created with BioGDP.com., figureFileSmall=NxVdMwjq4kGTmRFy6b/lgQ==, figureFileBig=RFH/vBMPjHUHDPtcngmoSQ==, tableContent=null), ArticleFig(id=1238891099658441098, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=CN, label=图6, caption=基于FRET原理的Mpro抑制剂筛选法, figureFileSmall=NxVdMwjq4kGTmRFy6b/lgQ==, figureFileBig=RFH/vBMPjHUHDPtcngmoSQ==, tableContent=null), ArticleFig(id=1238891099763298708, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=EN, label=Figure 7, caption=Screening of Mpro inhibitors based on the luciferase reporter screening assay^[83]. 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Structural domains and the active site of the coronavirus Mpro

, figureFileSmall=null, figureFileBig=null, tableContent=

Virus genus	Virus	Domain	Active site
α	HCoV-229E	Ⅰ (8-99), Ⅱ (100-183), long loop (184-199), Ⅲ (200-300)	His41 and Cys144[10-13]
	FIPV	-
	PEDV	-
	TGEV	Ⅰ (8-100), Ⅱ (101-183), long loop (184-199), Ⅲ (200-302)
β	MERS-CoV	Ⅰ (8-101), Ⅱ (102-184), long loop (185-200), Ⅲ (201-303)	His41 and Cys148[14]
	SARS-CoV		His41 and Cys145[15-16]
	SARS-CoV-2
γ	IBV	Ⅰ (3-99), Ⅱ (100-182), long loop (183-198), Ⅲ (199-307)	His41 and Cys143[17]
δ	PDCoV	Ⅰ (1-97), Ⅱ (98-186), long loop (187-199), Ⅲ (200-304)	His41 and Cys144[18]

), ArticleFig(id=1238891100618936782, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=CN, label=表1, caption=

冠状病毒Mpro结构域及活性位点

, figureFileSmall=null, figureFileBig=null, tableContent=

Virus genus	Virus	Domain	Active site
α	HCoV-229E	Ⅰ (8-99), Ⅱ (100-183), long loop (184-199), Ⅲ (200-300)	His41 and Cys144[10-13]
	FIPV	-
	PEDV	-
	TGEV	Ⅰ (8-100), Ⅱ (101-183), long loop (184-199), Ⅲ (200-302)
β	MERS-CoV	Ⅰ (8-101), Ⅱ (102-184), long loop (185-200), Ⅲ (201-303)	His41 and Cys148[14]
	SARS-CoV		His41 and Cys145[15-16]
	SARS-CoV-2
γ	IBV	Ⅰ (3-99), Ⅱ (100-182), long loop (183-198), Ⅲ (199-307)	His41 and Cys143[17]
δ	PDCoV	Ⅰ (1-97), Ⅱ (98-186), long loop (187-199), Ⅲ (200-304)	His41 and Cys144[18]

), ArticleFig(id=1238891100736377303, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=EN, label=Table 2, caption=

Analysis of host protein cleavage sites by coronavirus

, figureFileSmall=null, figureFileBig=null, tableContent=

Virus genus	Virus	Host protein	Cleavage site
α	HCoV-229E	NEMO[4]	Q83, Q205, and Q231
	FIPV	NEMO[53]	Q132, Q205, and Q231
	PEDV	NEMO[51] HDAC6[54]	Q231 Q519
	TGEV	HDAC6[54]	Q519
β	MERS-CoV	MAVS[55]	-
	SARS-CoV	NEMO[52]	E152, Q205, and Q231
	SARS-CoV-2	NEMO[52] RIG-I[56]	E152, Q205, and Q231 Q10
δ	PDCoV	NEMO[50] STAT2[57] IFIT3[58] HDAC6[54]	Q231 Q685 and Q758 Q406 Q519

), ArticleFig(id=1238891100887372263, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813312654299470, language=CN, label=表2, caption=

冠状病毒对宿主蛋白切割位点分析

, figureFileSmall=null, figureFileBig=null, tableContent=

Virus genus	Virus	Host protein	Cleavage site
α	HCoV-229E	NEMO[4]	Q83, Q205, and Q231
	FIPV	NEMO[53]	Q132, Q205, and Q231
	PEDV	NEMO[51] HDAC6[54]	Q231 Q519
	TGEV	HDAC6[54]	Q519
β	MERS-CoV	MAVS[55]	-
	SARS-CoV	NEMO[52]	E152, Q205, and Q231
	SARS-CoV-2	NEMO[52] RIG-I[56]	E152, Q205, and Q231 Q10
δ	PDCoV	NEMO[50] STAT2[57] IFIT3[58] HDAC6[54]	Q231 Q685 and Q758 Q406 Q519

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