ArticlePLoS pathogens2021
Acetylation of glucosyltransferases regulates Streptococcus mutans biofilm formation and virulence.
Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.
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Who cites it
35 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.
- Key virulence genes associated withFrontiers in oral health · 2025Pooled it
- High thrombin activity associated with crohn's disease induces microbiota pathogenicity contributing to mucosal inflammation.Gut microbes · 2026Article
- Dissecting the essential role ofVirulence · 2026Article
- Identification of a conserved GNAT-family lysine acetyltransferase inJournal of bacteriology · 2026Article
- Nicotinamide attenuates the virulence of colorectal cancer-associatedInfection and immunity · 2026Article
- Pyruvate metabolism is involved in adaptability and cariogenicity ofJournal of oral microbiology · 2026Review
- Crosstalk Between Lysine Lactylation and Acetylation Regulates Lactate Dehydrogenase in Streptococcus mutans.Genomics, proteomics & bioinformatics · 2025Article
- Trajectory and trends in molecular regulation ofFuture microbiology · 2025Article
- A novel selective medium Sucrose-Bacitracin agar 10 for accurate isolation and identification of Streptococcus mutans.BMC oral health · 2025Article
- Effects of a Novel Magnetic Nanomaterial on Oral Biofilms.International dental journal · 2025Article
- Time-resolved compositional and dynamics analysis of biofilm maturation and dispersal via solid-state NMR spectroscopy.NPJ biofilms and microbiomes · 2025Article
- Identification of the malonylation modification inFrontiers in microbiology · 2025Article
- Protein lysine acetylation regulates oral microorganisms.Frontiers in cellular and infection microbiology · 2025Review
- The role of universal stress protein Usp1413 in meropenem adaptive resistance and environmental stress responses inCurrent research in microbial sciences · 2025Article
- YkuR functions as a protein deacetylase inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification of ClpB, a molecular chaperone involved in the stress tolerance and virulence of Streptococcus agalactiae.Veterinary research · 2024Article
- Small RNA SmsR1 modulates acidogenicity and cariogenic virulence by affecting protein acetylation in Streptococcus mutans.PLoS pathogens · 2024Article
- SMU_1361c regulates the oxidative stress response ofApplied and environmental microbiology · 2024Article
- Article
- Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysine acetylation is a frequently occurring post-translational modification (PTM), emerging as an important metabolic regulatory mechanism in prokaryotes. This process is achieved enzymatically by the protein acetyltransferase (KAT) to specifically transfer the acetyl group, or non-enzymatically by direct intermediates (acetyl phosphate or acetyl-CoA). Although lysine acetylation modification of glucosyltransferases (Gtfs), the important virulence factor in Streptococcus mutans, was reported in our previous study, the KAT has not been identified. Here, we believe that the KAT ActG can acetylate Gtfs in the enzymatic mechanism. By overexpressing 15 KATs in S. mutans, the synthesized water-insoluble extracellular polysaccharides (EPS) and biofilm biomass were measured, and KAT (actG) was identified. The in-frame deletion mutant of actG was constructed to validate the function of actG. The results showed that actG could negatively regulate the water-insoluble EPS synthesis and biofilm formation. We used mass spectrometry (MS) to identify GtfB and GtfC as the possible substrates of ActG. This was also demonstrated by in vitro acetylation assays, indicating that ActG could increase the acetylation levels of GtfB and GtfC enzymatically and decrease their activities. We further found that the expression level of actG in part explained the virulence differences in clinically isolated strains. Moreover, overexpression of actG in S. mutans attenuated its cariogenicity in the rat caries model. Taken together, our study demonstrated that the KAT ActG could induce the acetylation of GtfB and GtfC enzymatically in S. mutans, providing insights into the function of lysine acetylation in bacterial virulence and pathogenicity.
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