Evidence map›Paper›PMID 30544243›Full record

ArticleNucleic acids research2019

A novel Staphylococcus aureus cis-trans type I toxin-antitoxin module with dual effects on bacteria and host cells.

Noëlla Germain-Amiot, Yoann Augagneur, Emilie Camberlein, Irène Nicolas, Valérie Lecureur, Astrid Rouillon, Brice Felden

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023
    Article
  6. Mechanism of action ofFrontiers in microbiology · 2023
    Article
  7. Thirty Years of sRNA-Mediated Regulation inInternational journal of molecular sciences · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. RNA Regulated Toxin-Antitoxin Systems in Pathogenic Bacteria.Frontiers in cellular and infection microbiology · 2021
    Review
  15. A peptide of a type I toxin-antitoxin system inducesProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Review
  17. Review
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Noëlla Germain-AmiotUniversité de Rennes 1, Inserm, BRM (Bacterial Regulatory RNAs and Medicine) UMR_S 1230, 35000 Rennes, France.
Yoann AugagneurUniversité de Rennes 1, Inserm, BRM (Bacterial Regulatory RNAs and Medicine) UMR_S 1230, 35000 Rennes, France.
Emilie CamberleinUniversité de Rennes 1, Inserm, BRM (Bacterial Regulatory RNAs and Medicine) UMR_S 1230, 35000 Rennes, France.
Irène NicolasUniversité de Rennes 1, Inserm, BRM (Bacterial Regulatory RNAs and Medicine) UMR_S 1230, 35000 Rennes, France.
Valérie LecureurUniversité de Rennes 1, CHU Rennes, Inserm, EHESP, Irset (Institut de recherche en santé, environnement et travail) UMR_S 1085, 35000 Rennes, France.
Astrid RouillonUniversité de Rennes 1, Inserm, BRM (Bacterial Regulatory RNAs and Medicine) UMR_S 1230, 35000 Rennes, France.
Brice FeldenUniversité de Rennes 1, Inserm, BRM (Bacterial Regulatory RNAs and Medicine) UMR_S 1230, 35000 Rennes, France.
Inserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial type I toxin-antitoxin (TA) systems are widespread, and consist of a stable toxic peptide whose expression is monitored by a labile RNA antitoxin. We characterized Staphylococcus aureus SprA2/SprA2AS module, which shares nucleotide similarities with the SprA1/SprA1AS TA system. We demonstrated that SprA2/SprA2AS encodes a functional type I TA system, with the cis-encoded SprA2AS antitoxin acting in trans to prevent ribosomal loading onto SprA2 RNA. We proved that both TA systems are distinct, with no cross-regulation between the antitoxins in vitro or in vivo. SprA2 expresses PepA2, a toxic peptide which internally triggers bacterial death. Conversely, although PepA2 does not affect bacteria when it is present in the extracellular medium, it is highly toxic to other host cells such as polymorphonuclear neutrophils and erythrocytes. Finally, we showed that SprA2AS expression is lowered during osmotic shock and stringent response, which indicates that the system responds to specific triggers. Therefore, the SprA2/SprA2AS module is not redundant with SprA1/SprA1AS, and its PepA2 peptide exhibits an original dual mode of action against bacteria and host cells. This suggests an altruistic behavior for S. aureus in which clones producing PepA2 in vivo shall die as they induce cytotoxicity, thereby promoting the success of the community.

Indexed as

Amino Acid SequenceBacterial ProteinsGene Expression Regulation, BacterialHost-Pathogen InteractionsHumansStaphylococcal InfectionsStaphylococcus aureusToxin-Antitoxin SystemsBacterial Proteins

Identifiers

PMID30544243
PMCPMC6393315
OpenAlexW2904113586

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.