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Lysine acetylation has been proven to play an important role in the virulence of <jats:italic>Streptococcus mutans<\/jats:italic>, a major cariogenic bacterial species. <jats:italic>S. mutans<\/jats:italic>\u2019 glucosyltransferases (Gtfs) are responsible for synthesizing extracellular polysaccharides (EPS) and contributing to biofilm formation. One of the most common nonsteroidal anti\u2010inflammatory drugs is acetylsalicylic acid (ASA), which can acetylate proteins through a nonenzymatic transacetylation reaction. Herein, we investigated the inhibitory effects of ASA on <jats:italic>S. mutans<\/jats:italic>. ASA treatment was observed to impede the growth of <jats:italic>S. mutans<\/jats:italic>, leading to a reduction in the production of water\u2010insoluble EPS and the formation of biofilm. Moreover, ASA decreased the enzyme activity of Gtfs while increasing the protein acetylation level. The in vivo anticaries efficacy of ASA has further been proved using the rat caries model. In conclusion, ASA as an acetylation agent attenuated the cariogenic virulence of <jats:italic>S. mutans<\/jats:italic>, suggesting the potential value of protein acetylation on antimicrobial and anti\u2010biofilm applications to <jats:italic>S. mutans<\/jats:italic>.<\/jats:p>","DOI":"10.1111\/omi.12452","type":"journal-article","created":{"date-parts":[[2024,1,15]],"date-time":"2024-01-15T15:25:10Z","timestamp":1705332310000},"page":"334-343","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Inhibition of <i>Streptococcus mutans<\/i> growth and biofilm formation through protein acetylation"],"prefix":"10.1111","volume":"39","author":[{"given":"Yongwang","family":"Lin","sequence":"first","affiliation":[{"name":"State Key Laboratory of Oral Diseases &amp; National Center for Stomatology &amp; National Clinical Research Center for Oral Diseases West China Hospital of Stomatology Sichuan University  Chengdu Sichuan 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