Evidence map›Paper›PMID 22027840›Full record

ArticleThe Journal of biological chemistry2011

Ultrahigh resolution and full-length pilin structures with insights for filament assembly, pathogenic functions, and vaccine potential.

Sophia Hartung, Andrew S Arvai, Timothy Wood, Subramaniapillai Kolappan, David S Shin, Lisa Craig, John A Tainer

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Article
  2. Type IV pili ofEcoSal Plus · 2024
    Review
  3. Article
  4. Understanding a Core Pilin of the Type IVa Pili ofJournal of microbiology and biotechnology · 2024
    Article
  5. Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. The structure of PilA fromThe Journal of biological chemistry · 2019
    Article
  16. DNA Uptake by Type IV Filaments.Frontiers in molecular biosciences · 2019
    Review
  17. Article
  18. A Pilin Region Affecting Host Range of theFrontiers in microbiology · 2018
    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

7 authors.

Sophia HartungLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Andrew S ArvaiDepartment of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037.
Timothy WoodDepartment of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037.
Subramaniapillai KolappanDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
David S ShinLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Lisa CraigDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada. Electronic address: licraig@sfu.ca.
John A TainerLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720; Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037. Electronic address: jatainer@lbl.gov.

Funding

Structure and Assembly of Type IV Pili &Related SystemsR01AI022160 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI TAINER, JOHN A. · 1985 to 2009
$3.2M
NIAID NIH HHS AI22160NIAID NIH HHS R01 AI022160
6 · The paper itself

Abstract

Pilin proteins assemble into Type IV pili (T4P), surface-displayed bacterial filaments with virulence functions including motility, attachment, transformation, immune escape, and colony formation. However, challenges in crystallizing full-length fiber-forming and membrane protein pilins leave unanswered questions regarding pilin structures, assembly, functions, and vaccine potential. Here we report pilin structures of full-length DnFimA from the sheep pathogen Dichelobacter nodosus and FtPilE from the human pathogen Francisella tularensis at 2.3 and 1 Å resolution, respectively. The DnFimA structure reveals an extended kinked N-terminal α-helix, an unusual centrally located disulfide, conserved subdomains, and assembled epitopes informing serogroup vaccines. An interaction between the conserved Glu-5 carboxyl oxygen and the N-terminal amine of an adjacent subunit in the crystallographic dimer is consistent with the hypothesis of a salt bridge between these groups driving T4P assembly. The FtPilE structure identifies an authentic Type IV pilin and provides a framework for understanding the role of T4P in F. tularensis virulence. Combined results define a unified pilin architecture, specialized subdomain roles in pilus assembly and function, and potential therapeutic targets.

Indexed as

Amino Acid SequenceBacterial ProteinsBacterial VaccinesCrystallography, X-RayDichelobacter nodosusFimbriae, BacterialFimbriae ProteinsModels, MolecularMolecular Sequence DataPolymersProtein ConformationSequence Homology, Amino AcidBacterial ProteinsBacterial VaccinesFimbriae ProteinsfimbrillinPolymers

Identifiers

PMID22027840
PMCPMC3243539

What OpenQuestion holds

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Registered trials

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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.