Evidence map›Paper›PMID 35978073›Full record

ArticleScientific reports2022

Streptococcus suis TrpX is part of a tryptophan uptake system, and its expression is regulated by a T-box regulatory element.

Muriel Dresen, Desirée Schaaf, Jesús Arenas, Astrid de Greeff, Peter Valentin-Weigand, Andreas Nerlich

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. 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
0.6field-weighted citation impact, top 31% 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, 3 citations in OpenAlex.

  1. Review
  2. Article
  3. Role of Metabolic Adaptation ofPathogens (Basel, Switzerland) · 2023
    Review
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 3 institutions in 3 countries.

Muriel DresenInstitute for Microbiology, University of Veterinary Medicine Hannover, Hannover, Germany. muriel.dresen@tiho-hannover.de.ORCID 0000-0002-2239-4683
Desirée SchaafInstitute for Microbiology, University of Veterinary Medicine Hannover, Hannover, Germany.ORCID 0000-0001-8072-2967
Jesús ArenasUnit of Microbiology and Immunology, Faculty of Veterinary, University of Zaragoza, Zaragoza, Spain.ORCID 0000-0002-8134-0693
Astrid de GreeffWageningen Bioveterinary Research, Part of Wageningen University and Research, Lelystad, The Netherlands.ORCID 0000-0002-2498-3668
Peter Valentin-WeigandInstitute for Microbiology, University of Veterinary Medicine Hannover, Hannover, Germany.ORCID 0000-0001-5411-6875
Andreas NerlichInstitute for Microbiology, University of Veterinary Medicine Hannover, Hannover, Germany.ORCID 0000-0001-8577-2744
University of Veterinary Medicine Hannover, Foundation · DEUniversidad de Zaragoza · ESWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus suis, a common member of the porcine respiratory microbiota, can cause life-threatening diseases in pigs as well as humans. A previous study identified the gene trpX as conditionally essential for in vivo survival by intrathecal infection of pigs with a transposon library of S. suis strain 10. Here, we characterized trpX, encoding a putative tryptophan/tyrosine transport system substrate-binding protein, in more detail. We compared growth capacities of the isogenic trpX-deficient mutant derivative strain 10∆trpX with its parent. Growth experiments in chemically defined media (CDM) revealed that growth of 10∆trpX depended on tryptophan concentration, suggesting TrpX involvement in tryptophan uptake. We demonstrated that trpX is part of an operon structure and co-transcribed with two additional genes encoding a putative permease and ATPase, respectively. Bioinformatics analysis identified a putative tryptophan T-box riboswitch in the 5' untranslated region of this operon. Finally, qRT-PCR and a reporter activation assay revealed trpX mRNA induction under tryptophan-limited conditions. In conclusion, our study showed that TrpX is part of a putative tryptophan ABC transporter system regulated by a T-box riboswitch probably functioning as a substrate-binding protein. Due to the tryptophan auxotrophy of S. suis, TrpX plays a crucial role for metabolic adaptation and growth during infection.

Indexed as

RiboswitchStreptococcal InfectionsStreptococcus suisAnimalsBacterial ProteinsBiological TransportCarrier ProteinsHumansOperonSwineTryptophanBacterial ProteinsCarrier ProteinsRiboswitchTryptophan

Identifiers

PMID35978073
PMCPMC9382623
OpenAlexW4292323911

What OpenQuestion holds

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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.