The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
The antimicrobial compound reuterin (3-hydroxypropionaldehyde) induces oxidative stress via interaction with thiol groups
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Reuterin is an antimicrobial compound produced by Lactobacillus reuteri, and has been proposed to mediate, in part, the probiotic health benefits ascribed to this micro-organism. Despite 20 years of investigation, the mechanism of action by which reuterin exerts its antimicrobial effects has remained elusive. Here we provide evidence that reuterin induces oxidative stress in cells, most likely by modifying thiol groups in proteins and small molecules. Escherichia coli cells subjected to sublethal levels of reuterin expressed a set of genes that overlapped with the set of genes composing the OxyR regulon, which senses and responds to various forms of oxidative stress. E. coli cells mutated for oxyR were more sensitive to reuterin compared with wild-type cells, further supporting a role for reuterin in exerting oxidative stress. The addition of cysteine to E. coli or Clostridium difficile growth media prior to exposure to reuterin suppressed the antimicrobial effect of reuterin on these bacteria. Interestingly, interaction with E. coli stimulated reuterin production or secretion by L. reuteri, indicating that contact with other microbes in the gut increases reuterin output. Thus, reuterin inhibits bacterial growth by modifying thiol groups, which indicates that reuterin negatively affects a large number of cellular targets.
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“In target organisms, reuterin can suppress ribonuclease activity [133,138] or induce oxidative stress by modifying thiol groups in proteins and glutathione [170].”
From Lactic Acid Bacteria in Raw-Milk Cheeses: From Starter Cultures to Probiotic Functions (2022) · cites this paper as [170]
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Flagged first, then by citations
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- Circle, 1945, Acrolein determination by means of tryptophan, Ind Eng Chem Res, 17, 259
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Metadata
- Authors
- Schaefer, L., Auchtung, T. A., Hermans, K. E., Whitehead, D., Borhan, B., & Britton, R. A.
- Affiliations
- Michigan State University (US)
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 2010-06-01
- Volume
- 156
- Issue
- 6
- Pages
- 1589-1599
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- PMC
- PMC7336520
- OpenAlex
- W2152598306
- Cited by
- 310
- References
- 42
- Citations by year
- 2026: 19 · 2025: 22 · 2024: 23 · 2023: 33 · 2022: 27 · 2021: 38 · 2020: 25 · 2019: 22 · 2018: 15 · 2017: 21 · 2016: 13 · 2015: 13 · 2014: 11 · 2013: 11 · 2012: 9
- FWCI
- 13.72
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Microbiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Gerber Foundation
- College of Engineering, Michigan State University
- National Institute of Allergy and Infectious Diseases (U19AI090872)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- reuterin, 3-hydroxypropionaldehyde, Lactobacillus reuteri, antimicrobial activity, oxidative stress, thiol modification, OxyR regulon, Escherichia coli, Clostridium difficile, cysteine, probiotics, gut microbiota
- MeSH terms
- Acrolein, Anti-Infective Agents, Bacteria, Escherichia coli, Glyceraldehyde, Hydro-Lyases, Propane, Repressor Proteins, Sulfhydryl Compounds, Oxidative Stress, Probiotics, Escherichia coli Proteins, Microbial Viability, Limosilactobacillus reuteri
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