ArticlePLoS pathogens2020
S-glutathionylation proteome profiling reveals a crucial role of a thioredoxin-like protein in interspecies competition and cariogenecity of Streptococcus mutans.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
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- MerR-type regulator ZccR links zinc homeostasis to biofilm formation and interspecies competition inFrontiers in cellular and infection microbiology · 2026Article
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- Trajectory and trends in molecular regulation ofFuture microbiology · 2025Article
- A Narrative Review of the Role of S-Glutathionylation in Bacteria.Microorganisms · 2025Review
- Streptococcus mutans regulates ubiquitin modification of Candida albicans in the bacterial-fungal interaction.PLoS pathogens · 2025Article
- Longitudinal Microbiome Changes in Supragingival Biofilm Transcriptomes Induced by Orthodontics.JDR clinical and translational research · 2024Article
- Small RNA SmsR1 modulates acidogenicity and cariogenic virulence by affecting protein acetylation in Streptococcus mutans.PLoS pathogens · 2024Article
- Oxidative stress response: a critical factor affecting the ecological competitiveness ofJournal of oral microbiology · 2024Review
- Thioredoxin A of Streptococcus suis Serotype 2 Contributes to Virulence by Inhibiting the Expression of Pentraxin 3 to Promote Survival Within Macrophages.Journal of microbiology (Seoul, Korea) · 2023Article
- Regulatory mechanisms of exopolysaccharide synthesis and biofilm formation in Streptococcus mutans.Journal of oral microbiology · 2023Review
- Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.Antioxidants (Basel, Switzerland) · 2022Review
- Targeting the YXXΦ Motifs of the SARS Coronaviruses 1 and 2 ORF3a Peptides by In Silico Analysis to Predict Novel Virus-Host Interactions.Biomolecules · 2022Article
- SiteMotif: A graph-based algorithm for deriving structural motifs in Protein Ligand binding sites.PLoS computational biology · 2022Article
- Nicotinamide could reduce growth and cariogenic virulence ofJournal of oral microbiology · 2022Article
- Systematic analysis of lysine malonylation inFrontiers in cellular and infection microbiology · 2022Article
- Acetylation of glucosyltransferases regulates Streptococcus mutans biofilm formation and virulence.PLoS pathogens · 2021Article
- New roles for glutathione: Modulators of bacterial virulence and pathogenesis.Redox biology · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
S-glutathionylation is an important post-translational modification (PTM) process that targets protein cysteine thiols by the addition of glutathione (GSH). This modification can prevent proteolysis caused by the excessive oxidation of protein cysteine residues under oxidative or nitrosative stress conditions. Recent studies have suggested that protein S-glutathionylation plays an essential role in the control of cell-signaling pathways by affecting the protein function in bacteria and even humans. In this study, we investigated the effects of S-glutathionylation on physiological regulation within Streptococcus mutans, the primary etiological agent of human dental caries. To determine the S-glutathionylated proteins in bacteria, the Cys reactive isobaric reagent iodoacetyl Tandem Mass Tag (iodoTMT) was used to label the S-glutathionylated Cys site, and an anti-TMT antibody-conjugated resin was used to enrich the modified peptides. Proteome profiling identified a total of 357 glutathionylated cysteine residues on 239 proteins. Functional enrichment analysis indicated that these S-glutathionylated proteins were involved in diverse important biological processes, such as pyruvate metabolism and glycolysis. Furthermore, we studied a thioredoxin-like protein (Tlp) to explore the effect of S-glutathionylation on interspecies competition between oral streptococcal biofilms. Through site mutagenesis, it was proved that glutathionylation on Cys41 residue of Tlp is crucial to protect S. mutans from oxidative stress and compete with S. sanguinis and S. gordonii. An addition rat caries model showed that the loss of S-glutathionylation attenuated the cariogenicity of S. mutans. Taken together, our study provides an insight into the S-glutathionylation of bacterial proteins and the regulation of oxidative stress resistance and interspecies competition.
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