Evidence map›Paper›PMID 37183214›Full record

ArticleMedical microbiology and immunology2023

Trimer stability of Helicobacter pylori HtrA is regulated by a natural mutation in the protease domain.

Urszula Zarzecka, Nicole Tegtmeyer, Heinrich Sticht, Steffen Backert

Open access · hybridAbstract read
In one paragraph

Article in Medical microbiology and immunology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
6.0field-weighted citation impact, top 3% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

  1. Pooled it
  2. Host andGut microbes · 2026
    Article
  3. Distinct Modulation ofBiomolecules · 2026
    Article
  4. Article
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  6. Resistome and virulome determination inMicrobiology spectrum · 2025
    Article
  7. Therapeutic and protective approaches to combatFrontiers in pharmacology · 2025
    Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Clinical Pathogenesis, Molecular Mechanisms of Gastric Cancer Development.Current topics in microbiology and immunology · 2023
    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

4 authors at 1 institution in 2 countries.

Urszula ZarzeckaDivision of Microbiology, Department of Biology, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
Nicole TegtmeyerDivision of Microbiology, Department of Biology, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
Heinrich StichtDivision of Bioinformatics, Institute of Biochemistry, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
Steffen BackertDivision of Microbiology, Department of Biology, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany. Steffen.Backert@fau.de.ORCID http://orcid.org/0000-0002-8948-8254
Friedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

Bundesministerium für Bildung und Forschung IP9/ 01KI2007E
6 · The paper itself

Abstract

The human pathogen Helicobacter pylori is a major risk factor for gastric disease development. Serine protease HtrA is an important bacterial virulence factor that cleaves the cell junction proteins occludin, claudin-8 and E-cadherin, which causes gastric tissue damage. Using casein zymography, we discovered that HtrA trimer stability varies in clinical H. pylori strains. Subsequent sequence analyses revealed that HtrA trimer stability correlated with the presence of leucine or serine residue at position 171. The importance of these amino acids in determining trimer stability was confirmed by leucine-to-serine swapping experiments using isogenic H. pylori mutant strains as well as recombinant HtrA proteins. In addition, this sequence position displays a high sequence variability among various bacterial species, but generally exhibits a preference for hydrophilic amino acids. This natural L/S171 polymorphism in H. pylori may affect the protease activity of HtrA during infection, which could be of clinical importance and may determine gastric disease development.

Indexed as

Helicobacter pyloriBacterial ProteinsHumansLeucineMutationRecombinant ProteinsSerineSerine ProteasesBacterial ProteinsLeucineRecombinant ProteinsSerineSerine ProteasesHelicobacter pyloriHtrAProteasesTrimer stability

Identifiers

PMID37183214
PMCPMC10293373
OpenAlexW4376630042

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.