Evidence map›Paper›PMID 18583342›Full record

ArticleThe Journal of biological chemistry2008

Oligomerization of PcrV and LcrV, protective antigens of Pseudomonas aeruginosa and Yersinia pestis.

Caroline Gébus, Gébus Caroline, Eric Faudry, Faudry Eric, Yu-Sing Tammy Bohn, Sylvie Elsen, Elsen Sylvie, Ina Attree

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mechanistic blockade ofAntimicrobial agents and chemotherapy · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Caroline, Gébus [corrected to Gébus, Caroline]; Eric, Faudry [corrected to Faudry, Eric]; Sylvie, Elsen [corrected to Elsen, Sylvie]
5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Caroline GébusLaboratoire de Biochimie et Biophysique des Systèmes Intégrés (Unité mixte de recherche 5092), CNRS, Université Joseph Fourier, Commissariat à l'Energie Atomique, DSV, iRTSV, 17 rue des Martyrs, Grenoble, France.
Gébus Caroline
Eric Faudry
Faudry Eric
Yu-Sing Tammy Bohn
Sylvie Elsen
Elsen Sylvie
Ina Attree
Université Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protective antigens of Pseudomonas aeruginosa (PcrV) and Yersinia pestis (LcrV) are key elements of specialized machinery, the type III secretion system (T3SS), which enables the injection of effector molecules into eukaryotic cells. Being positioned at the injectisome extremity, V proteins participate in the translocation process across the host cell plasma membrane. In this study, we demonstrate the assembly of V proteins into oligomeric doughnut-like complexes upon controlled refolding of the proteins in vitro. The oligomeric nature of refolded PcrV was revealed by size exclusion chromatography, native gel electrophoresis, and native mass spectrometry, which ascertain the capacity of the protein to multimerize into higher-order species. Furthermore, transmission electron microscopy performed on oligomers of both PcrV and LcrV revealed the presence of distinct structures with approximate internal and external diameters of 3-4 and 8-10 nm, respectively. The C-terminal helix, alpha12, of PcrV and notably the hydrophobic residues Val(255), Leu(262), and Leu(276) located within this helix, were shown to be crucial for oligomerization. Moreover, the corresponding mutant proteins produced in P. aeruginosa were found to be non-functional in in vivo type III-dependent cytotoxicity assays by directly affecting the correct assembly of PopB/D translocon within the host cell membranes. The detailed understanding of structure-function relationships of T3SS needle tip proteins will be of value in further developments of new vaccines and antimicrobials.

Indexed as

AnimalsAntigens, BacterialAnti-Infective AgentsBacterial ToxinsBacterial VaccinesDrug DesignHydrophobic and Hydrophilic InteractionsMacrophagesMiceMultiprotein ComplexesMutationPlaguePore Forming Cytotoxic ProteinsProtein FoldingProtein Structure, QuaternaryProtein Structure, SecondaryAntigens, Bacterialantigen V, PseudomonasAnti-Infective AgentsBacterial ToxinsBacterial VaccinesLcrV protein, YersiniaMultiprotein ComplexesPore Forming Cytotoxic Proteins

Identifiers

PMID18583342
PMCPMC3259777
OpenAlexW2097099366

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.