Evidence map›Paper›PMID 17921300›Full record

ArticleJournal of bacteriology2007

A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport.

Ulrike Grosskinsky, Monika Schütz, Michaela Fritz, Yvonne Schmid, Marina C Lamparter, Pawel Szczesny, Andrei N Lupas, Ingo B Autenrieth, Dirk Linke

Abstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

43 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Comparative genomics andFrontiers in microbiology · 2026
    Article
  3. Article
  4. Recombinant Expression and Overproduction of Transmembrane β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Aptasensor for the Detection ofBioengineering (Basel, Switzerland) · 2023
    Article
  6. Article
  7. Identification of the adhesive domain of AtaA fromFrontiers in bioengineering and biotechnology · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. The Trimeric Autotransporter Adhesin YadA ofFrontiers in microbiology · 2021
    Article
  12. CEACAM1 Activation by CbpF-ExpressingFrontiers in cellular and infection microbiology · 2021
    Article
  13. Article
  14. BamA is required for autotransporter secretion.Biochimica et biophysica acta. General subjects · 2020
    Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Bacterial autoaggregation.AIMS microbiology · 2018
    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.

Ulrike GrosskinskyInstitut für Medizinische Mikrobiologie und Hygiene, Universitätsklinikum Tübingen, Tübingen, Germany.
Monika Schütz
Michaela Fritz
Yvonne Schmid
Marina C Lamparter
Pawel Szczesny
Andrei N Lupas
Ingo B Autenrieth
Dirk Linke
Universitätsklinikum Tübingen · DEMax Planck Institute for Developmental Biology · DEInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Yersinia adhesin A (YadA) is a trimeric autotransporter adhesin of enteric yersiniae. It consists of three major domains: a head mediating adherence to host cells, a stalk involved in serum resistance, and an anchor that forms a membrane pore and is responsible for the autotransport function. The anchor contains a glycine residue, nearly invariant throughout trimeric autotransporter adhesins, that faces the pore lumen. To address the role of this glycine, we replaced it with polar amino acids of increasing side chain size and expressed wild-type and mutant YadA in Escherichia coli. The mutations did not impair the YadA-mediated adhesion to collagen and to host cells or the host cell cytokine production, but they decreased the expression levels and stability of YadA trimers with increasing side chain size. Likewise, autoagglutination and resistance to serum were decreased in these mutants. We found that the periplasmic protease DegP is involved in the degradation of YadA and that in an E. coli degP deletion strain, mutant versions of YadA were expressed almost to wild-type levels. We conclude that the conserved glycine residue affects both the export and the stability of YadA and consequently some of its putative functions in pathogenesis.

Indexed as

Adhesins, BacterialAmino Acid SubstitutionBacterial AdhesionCollagenConserved SequenceEscherichia coliGene DeletionGene ExpressionGlycineHeat-Shock ProteinsHeLa CellsHumansMicrobial ViabilityMutagenesis, Site-DirectedPeriplasmic ProteinsProtein BindingAdhesins, BacterialCollagenDegP proteaseGlycineHeat-Shock ProteinsPeriplasmic ProteinsSerine EndopeptidasesYadA protein, Yersinia

Identifiers

PMID17921300
PMCPMC2168626
OpenAlexW1984580868

What OpenQuestion holds

Textmetadata
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.