ArticleScientific reports2017
Remodeling of the Streptococcus mutans proteome in response to LrgAB and external stresses.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Selenite tolerance, reduction performance and biogenic selenium nanoparticle biosynthesis by Priestia aryabhattai YL286 isolated from the wheat phyllosphere.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Article
- A Scorecard for Information Synthesis in Multiple Experimental Conditions: Application to Bacterial Biofilm Matrix Transcriptomics.Current microbiology · 2025Article
- Transcriptome analysis of tilapia streptococcus agalactiae in response to baicalin.Genes & genomics · 2025Article
- NovoLign: metaproteomics by sequence alignment.ISME communications · 2024Article
- Regulation of cid and lrg expression by CodY in Streptococcus mutans.MicrobiologyOpen · 2020Article
- Peptides encoded in theMicrobiology (Reading, England) · 2020Article
- Environmental Triggers ofFrontiers in microbiology · 2020Article
- Understanding LrgAB Regulation ofFrontiers in microbiology · 2020Article
- Immune Responses to Gram-Negative Bacteria in Hemolymph of the Chinese Horseshoe Crab,Frontiers in immunology · 2020Article
- Characterization of LrgAB as a stationary phase-specific pyruvate uptake system in Streptococcus mutans.BMC microbiology · 2019Article
- Inactivation ofJournal of oral microbiology · 2019Article
- Regulation of cid and lrg expression by CcpA in Streptococcus mutans.Microbiology (Reading, England) · 2019Article
- Transcriptome and Proteome of Fish-PathogenicFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Streptococcus mutans Cid/Lrg system represents an ideal model to study how this organism withstands various stressors encountered in the oral cavity. Mutation of lrgAB renders S. mutans more sensitive to oxidative, heat, and vancomycin stresses. Here, we have performed a comprehensive proteomics experiment using label-free quantitative mass spectrometry to compare the proteome changes of wild type UA159 and lrgAB mutant strains in response to these same stresses. Importantly, many of identified proteins showed either a strikingly large fold-change, or were completely suppressed or newly induced in response to a particular stress condition. Notable stress proteome changes occurred in a variety of functional categories, including amino acid biosynthesis, energy metabolism, protein synthesis, transport/binding, and transcriptional/response regulators. In the non-stressed growth condition, mutation of lrgAB significantly altered the abundance of 76 proteins (a fold change >1.4, or <0.6, p-value <0.05) and several of these matched the stress proteome of the wild type strain. Interestingly, the statistical correlation between the proteome changes and corresponding RNA-seq transcriptomic studies was relatively low (rho(ρ) <0.16), suggesting that adaptation to a new environment may require radical proteome turnover or metabolic remodeling. Collectively, this study reinforces the importance of LrgAB to the S. mutans stress response.
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