Tea Catechins in Green Tea Inhibit the Activity of SARS-CoV-2 Main Protease via Covalent Adduction

IF 5.7 1区农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY

Journal of Agricultural and Food Chemistry Pub Date : 2025-02-05 DOI:10.1021/acs.jafc.4c11685

Yoji Kato, Sakiko Suzuki, Akari Higashiyama, Ichiro Kaneko, Mitsugu Akagawa, Miyu Nishikawa, Shinichi Ikushiro

{"title":"Tea Catechins in Green Tea Inhibit the Activity of SARS-CoV-2 Main Protease via Covalent Adduction","authors":"Yoji Kato, Sakiko Suzuki, Akari Higashiyama, Ichiro Kaneko, Mitsugu Akagawa, Miyu Nishikawa, Shinichi Ikushiro","doi":"10.1021/acs.jafc.4c11685","DOIUrl":null,"url":null,"abstract":"We herein examined the inhibitory effects of tea catechins on the SARS-CoV-2 main protease (Mpro). Among the catechins analyzed, epigallocatechin 3-(3″-O-methyl)gallate, epigallocatechin gallate (EGCG), gallocatechin, gallocatechin gallate, and epigallocatechin inhibited recombinant Mpro in a dose-dependent manner. Peptide mapping revealed that catechins preferentially formed covalent bonds with five sequences with the strongest activity at the C145 active site. Fragmentation analysis indicated 184 cleavages from peptides containing C145, corresponding to the D ring, suggesting that the B ring was attached to C145. When 10 bottled teas were incubated with Mpro, four green teas inhibited the enzyme by over 80%, whereas the blended and barley teas showed no effect. EGCG reacted covalently with SARS-CoV-2 Mpro within cells when incubated with cultured cells expressing Mpro. This is the first study to report direct covalent binding between tea catechins and Mpro in cells. This suggests that catechins from green tea can inhibit Mpro in infected cells.","PeriodicalId":41,"journal":{"name":"Journal of Agricultural and Food Chemistry","volume":"37 1","pages":""},"PeriodicalIF":5.7000,"publicationDate":"2025-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Agricultural and Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1021/acs.jafc.4c11685","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}

引用次数: 0

Abstract

We herein examined the inhibitory effects of tea catechins on the SARS-CoV-2 main protease (M^pro). Among the catechins analyzed, epigallocatechin 3-(3″-O-methyl)gallate, epigallocatechin gallate (EGCG), gallocatechin, gallocatechin gallate, and epigallocatechin inhibited recombinant M^pro in a dose-dependent manner. Peptide mapping revealed that catechins preferentially formed covalent bonds with five sequences with the strongest activity at the C145 active site. Fragmentation analysis indicated 184 cleavages from peptides containing C145, corresponding to the D ring, suggesting that the B ring was attached to C145. When 10 bottled teas were incubated with M^pro, four green teas inhibited the enzyme by over 80%, whereas the blended and barley teas showed no effect. EGCG reacted covalently with SARS-CoV-2 M^pro within cells when incubated with cultured cells expressing M^pro. This is the first study to report direct covalent binding between tea catechins and M^pro in cells. This suggests that catechins from green tea can inhibit M^pro in infected cells.

Abstract Image

查看原文本刊更多论文

求助全文

约1分钟内获得全文求助全文

来源期刊

Journal of Agricultural and Food Chemistry 农林科学-农业综合

CiteScore

9.90

自引率

8.20%

发文量

1375

审稿时长

2.3 months

期刊介绍： The Journal of Agricultural and Food Chemistry publishes high-quality, cutting edge original research representing complete studies and research advances dealing with the chemistry and biochemistry of agriculture and food. The Journal also encourages papers with chemistry and/or biochemistry as a major component combined with biological/sensory/nutritional/toxicological evaluation related to agriculture and/or food.