Evidence map›Paper›PMID 23687270›Full record

ArticleJournal of bacteriology2013

Structural basis for biofilm formation via the Vibrio cholerae matrix protein RbmA.

Krista M Giglio, Jiunn C Fong, Fitnat H Yildiz, Holger Sondermann

Abstract 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 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
–field-weighted citation impact
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

54 citing papers in PubMed.

  1. Article
  2. Structural basis of biofilm formation mediated by thebioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Non-O1/Non-O139Microorganisms · 2024
    Review
  12. Review
  13. Article
  14. Article
  15. Breakdown of clonal cooperative architecture in multispecies biofilms and the spatial ecology of predation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Krista M GiglioDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA.
Jiunn C Fong
Fitnat H Yildiz
Holger Sondermann

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Smooth to Rugose phase variation in Vibrio choleraeR01AI055987 · NIAID · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI YILDIZ, HAVVA FITNAT · 2003 to 2019
$4.4M
Molecular mechanism regulating periplasmic proteolysis in bacterial pathogenesisR01AI097307 · NIAID · CORNELL UNIVERSITY · PI O'TOOLE, GEORGE A., SONDERMANN, HOLGER · 2012 to 2016
$1.9M
NIAID NIH HHS R01 AI055987NIAID NIH HHS R01-AI055987NIAID NIH HHS R01 AI097307NIAID NIH HHS R01-AI097307NIGMS NIH HHS DMR-0225180NIGMS NIH HHS GM103485NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

During the transition from a free-swimming, single-cell lifestyle to a sessile, multicellular state called a biofilm, bacteria produce and secrete an extracellular matrix comprised of nucleic acids, exopolysaccharides, and adhesion proteins. The Vibrio cholerae biofilm matrix contains three major protein components, RbmA, Bap1, and RbmC, which are unique to Vibrio cholerae and appear to support biofilm formation at particular steps in the process. Here, we focus on RbmA, a structural protein with an unknown fold. RbmA participates in the early cell-cell adhesion events and is found throughout the biofilm where it localizes to cell-cell contact sites. We determined crystal structures of RbmA and revealed that the protein folds into tandem fibronectin type III (FnIII) folds. The protein is dimeric in solution and in crystals, with the dimer interface displaying a surface groove that is lined with several positively charged residues. Structure-guided mutagenesis studies establish a crucial role for this surface patch for RbmA function. On the basis of the structure, we hypothesize that RbmA serves as a tether by maintaining flexible linkages between cells and the extracellular matrix.

Indexed as

Adhesins, BacterialBacterial AdhesionBacterial ProteinsBiofilmsCrystallography, X-RayDNA Mutational AnalysisModels, MolecularMutagenesisProtein ConformationProtein FoldingProtein MultimerizationVibrio choleraeAdhesins, BacterialBacterial Proteins

Identifiers

PMID23687270
PMCPMC3697633

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.