Evidence map›Paper›PMID 34493209›Full record

ArticleBMC genomics2021

Redox proteomic study of Bacillus cereus thiol proteome during fermentative anaerobic growth.

Fella Hamitouche, Jean-Charles Gaillard, Philippe Schmitt, Jean Armengaud, Catherine Duport, Luc Dedieu

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Cysteine Proteome Reveals Response to Endogenous Oxidative Stress inInternational journal of molecular sciences · 2021
    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

6 authors at 4 institutions in 1 country.

Fella HamitoucheAvignon Université, INRAE, UMR SQPOV, Site Agroparc, F-84914, Avignon Cedex 9, France.
Jean-Charles GaillardUniversité Paris-Saclay, CEA, INRAE, Département Médicaments et Technologies pour la Santé (DMTS), SPI, 30200, Bagnols-sur-Cèze, France.
Philippe SchmittAvignon Université, INRAE, UMR SQPOV, Site Agroparc, F-84914, Avignon Cedex 9, France.
Jean ArmengaudUniversité Paris-Saclay, CEA, INRAE, Département Médicaments et Technologies pour la Santé (DMTS), SPI, 30200, Bagnols-sur-Cèze, France.
Catherine Duport *Avignon Université, INRAE, UMR SQPOV, Site Agroparc, F-84914, Avignon Cedex 9, France.
Luc Dedieu *Avignon Université, INRAE, UMR SQPOV, Site Agroparc, F-84914, Avignon Cedex 9, France. luc.dedieu@univ-avignon.fr.
Université d'Avignon et des Pays de Vaucluse · FRCEA Paris-Saclay · FRInstitut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FRSécurité et Qualité des Produits d'Origine Végétale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBacillus cereus is a notorious foodborne pathogen, which can grow under anoxic conditions. Anoxic growth is supported by endogenous redox metabolism, for which the thiol redox proteome serves as an interface. Here, we studied the cysteine (Cys) proteome dynamics of B. cereus ATCC 14579 cells grown under fermentative anoxic conditions. We used a quantitative thiol trapping method combined with proteomics profiling.

resultsIn total, we identified 153 reactive Cys residues in 117 proteins participating in various cellular processes and metabolic pathways, including translation, carbohydrate metabolism, and stress response. Of these reactive Cys, 72 were detected as reduced Cys. The B. cereus Cys proteome evolved during growth both in terms of the number of reduced Cys and the Cys-containing proteins identified, reflecting its growth-phase-dependence. Interestingly, the reduced status of the B. cereus thiol proteome increased during growth, concomitantly to the decrease of extracellular oxidoreduction potential.

conclusionsTaken together, our data show that the B. cereus Cys proteome during unstressed fermentative anaerobic growth is a dynamic entity and provide an important foundation for future redox proteomic studies in B. cereus and other organisms.

Indexed as

Bacillus cereusProteomeAnaerobiosisOxidation-ReductionProteomicsSulfhydryl CompoundsProteomeSulfhydryl CompoundsAnaerobiosisBacillus cereusDifferential labeling strategyFermentative growthThiol proteome

Identifiers

PMID34493209
PMCPMC8425097
OpenAlexW3197484858

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.