Evidence map›Paper›PMID 24358297›Full record

ArticlePloS one2013

The sodium/proline transporter PutP of Helicobacter pylori.

Araceli Rivera-Ordaz, Susanne Bracher, Sannia Sarrach, Zheng Li, Lei Shi, Matthias Quick, Daniel Hilger, Rainer Haas, Heinrich Jung

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Challenges and Prospects for Eradication ofPathogens (Basel, Switzerland) · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. 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

9 authors at 3 institutions in 2 countries.

Araceli Rivera-OrdazMicrobiology, Department of Biology I, Ludwig Maximilians University Munich, Martinsried, Germany.
Susanne BracherMicrobiology, Department of Biology I, Ludwig Maximilians University Munich, Martinsried, Germany.
Sannia SarrachMicrobiology, Department of Biology I, Ludwig Maximilians University Munich, Martinsried, Germany.
Zheng LiDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, United States of America.
Lei ShiDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, United States of America ; HRH Prince Alwaleed Bin Talal Bin Abdulaziz Alsaud Institute for Computational Biomedicine, Weill Cornell Medical College, New York, New York, United States of America.
Matthias QuickCenter for Molecular Recognition and Department of Psychiatry, Columbia University College of Physicians and Surgeons, New York, New York, United States of America.
Daniel HilgerMicrobiology, Department of Biology I, Ludwig Maximilians University Munich, Martinsried, Germany.
Rainer HaasMax von Pettenkofer Institute for Hygiene and Medical Microbiology, Ludwig Maximilians University Munich, Munich, Germany.
Heinrich JungMicrobiology, Department of Biology I, Ludwig Maximilians University Munich, Martinsried, Germany.
Ludwig-Maximilians-Universität München · DECornell University · USColumbia University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Helicobacter pylori is cause of chronic gastritis, duodenal ulcer and gastric carcinoma in humans. L-proline is a preferred energy source of the microaerophilic bacterium. Previous analyses revealed that HpputP and HpputA, the genes that are predicted to play a central role in proline metabolism as they encode for the proline transporter and proline dehydrogenase, respectively, are essential for stomach colonization. Here, the molecular basis of proline transport in H. pylori by HpPutP was investigated experimentally for the first time. Measuring radiolabeled substrate transport in H. pylori and E. coli heterologously expressing HpputP as well as in proteoliposomes reconstituted with HpPutP, we demonstrate that the observed proline transport in H. pylori is mediated by HpPutP. HpPutP is specific and exhibits a high affinity for L-proline. Notably, L-proline transport is exclusively dependent on Na(+) as coupling ion, i.e., Na(+)/L-proline symport, reminiscent to the properties of PutP of E. coli even though H. pylori lives in a more acidic environment. Homology model-based structural comparisons and substitution analyses identified amino acids crucial for function. HpPutP-catalyzed proline uptake was efficiently inhibited by the known proline analogs 3,4-dehydro-D,L-proline and L-azetidine-2-carboxylic acid.

Indexed as

Amino Acid Transport Systems, NeutralBinding SitesBiological TransportEscherichia coli ProteinsHelicobacter pyloriModels, MolecularProlineSequence HomologySodiumStructure-Activity RelationshipSymportersAmino Acid Transport Systems, NeutralEscherichia coli ProteinsProlinePutP protein, E coliSodiumSymporters

Identifiers

PMID24358297
PMCPMC3866251
OpenAlexW2090417273

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.