Evidence map›Paper›PMID 24123820›Full record

ArticleJournal of bacteriology2013

Structural and population characterization of MrkD, the adhesive subunit of type 3 fimbriae.

Steen G Stahlhut, Sujay Chattopadhyay, Dagmara I Kisiela, Kristian Hvidtfeldt, Steven Clegg, Carsten Struve, Evgeni V Sokurenko, Karen A Krogfelt

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Virulence Factors inIndian journal of microbiology · 2024
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Turn Up the Heat-Food and ClinicalFrontiers in microbiology · 2017
    Article
  15. Review
  16. Article
  17. Article
  18. 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

8 authors at 3 institutions in 2 countries.

Steen G StahlhutDepartment of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark.
Sujay Chattopadhyay
Dagmara I Kisiela
Kristian Hvidtfeldt
Steven Clegg
Carsten Struve
Evgeni V Sokurenko
Karen A Krogfelt
Statens Serum Institut · DKUniversity of Washington · USUniversity of Iowa · US

Funding

Pathogenesis of Klebsiells airway infectionsR01AI050011 · NIAID · UNIVERSITY OF IOWA · PI CLEGG, STEVEN · 2003 to 2010
$2.2M
NIAID NIH HHS R01 AI050011NIAID NIH HHS R01-AI50011
6 · The paper itself

Abstract

Type 3 fimbriae are adhesive organelles found in enterobacterial pathogens. The fimbriae promote biofilm formation on biotic and abiotic surfaces; however, the exact identity of the receptor for the type 3 fimbriae adhesin, MrkD, remains elusive. We analyzed naturally occurring structural and functional variabilities of the MrkD adhesin from Klebsiella pneumoniae and Escherichia coli isolates of diverse origins. We identified a total of 33 allelic variants of mrkD among 90 K. pneumoniae isolates and 10 allelic variants among 608 E. coli isolates, encoding 11 and 9 protein variants, respectively. Based on the level of accumulated silent variability between the alleles, mrkD was acquired a relatively long time ago in K. pneumoniae but recently in E. coli. However, unlike K. pneumoniae, mrkD in E. coli is actively evolving under a strong positive selection by accumulation of mutations, often targeting the same positions in the protein. Several naturally occurring MrkD protein variants from E. coli were found to be significantly less adherent when tested in a mannan-binding assay and showed reduced biofilm-forming capacity. Functional examination of the MrkD adhesin in flow chamber experiments determined that it interacts with Saccharomyces cerevisiae cells in a shear-dependent manner, i.e., the binding is catch-bond-like and enhanced under increasing shear conditions. Homology modeling strongly suggested that MrkD has a two-domain structure, comprising a pilin domain anchoring the adhesin to the fimbrial shaft and a lectin domain containing the binding pocket; this is similar to structures found in other catch-bond-forming fimbrial adhesins in enterobacteria.

Indexed as

Bacterial AdhesionAdhesins, BacterialAdhesins, Escherichia coliAllelesBiofilmsDNA, BacterialEscherichia coliEscherichia coli ProteinsFimbriae ProteinsGenetic VariationKlebsiella pneumoniaeMicrobial InteractionsModels, MolecularMolecular Sequence DataMutation, MissenseProtein ConformationAdhesins, BacterialAdhesins, Escherichia coliDNA, BacterialEscherichia coli ProteinsFimbriae ProteinsKlebsiella pneumoniae type 3 fimbrial adhesinMrkD protein, E coli

Identifiers

PMID24123820
PMCPMC3889607
OpenAlexW2117512031

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.