Evidence map›Paper›PMID 19815547›Full record

ArticleThe Journal of biological chemistry2009

HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor.

Véronique Viarre, Eric Cascales, Geneviève Ball, Gérard P F Michel, Alain Filloux, Romé Voulhoux

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Secrete or perish: The role of secretion systems inComputational and structural biotechnology journal · 2021
    Review
  4. Article
  5. Article
  6. Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Membrane-Bound PenA β-Lactamase of Burkholderia pseudomallei.Antimicrobial agents and chemotherapy · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Editorial.FEMS microbiology reviews · 2015
    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

6 authors at 2 institutions in 2 countries.

Véronique ViarreLaboratoire d'Ingénierie des Systèmes Macromoléculaires (UPR 9027), CNRS, Institut de Microbiologie de la Méditerranée, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
Eric Cascales
Geneviève Ball
Gérard P F Michel
Alain Filloux
Romé Voulhoux
Centre National de la Recherche Scientifique · FRInstitut de Microbiologie de la Méditerranée · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretins are an unusual and important class of bacterial outer membrane (OM) proteins. They are involved in the transport of single proteins or macromolecular structures such as pili, needle complexes, and bacteriophages across the OM. Secretins are multimeric ring-shaped structures that form large pores in the OM. The targeting of such macromolecular structures to the OM often requires special assistance, conferred by specific pilotins or pilot proteins. Here, we investigated HxcQ, the OM component of the second Pseudomonas aeruginosa type II secretion system. We found that HxcQ forms high molecular mass structures resistant to heat and SDS, revealing its secretin nature. Interestingly, we showed that HxcQ is a lipoprotein. Construction of a recombinant nonlipidated HxcQ (HxcQnl) revealed that lipidation is essential for HxcQ function. Further phenotypic analysis indicated that HxcQnl accumulates as multimers in the inner membrane of P. aeruginosa, a typical phenotype observed for secretins in the absence of their cognate pilotin. Our observations led us to the conclusion that the lipid anchor of HxcQ plays a pilotin role. The self-piloting of HxcQ to the OM was further confirmed by its correct multimeric OM localization when expressed in the heterologous host Escherichia coli. Altogether, our results reveal an original and unprecedented pathway for secretin transport to the OM.

Indexed as

Bacterial Outer Membrane ProteinsBiological TransportCentrifugation, Density GradientDetergentsEscherichia coliLipidsLipoproteinsPalmitic AcidPeptidesPlasmidsProtein Structure, TertiaryPseudomonas aeruginosaSecretinBacterial Outer Membrane ProteinsDetergentsglobomycinLipidsLipoproteinsPalmitic AcidPeptidesSecretin

Identifiers

PMID19815547
PMCPMC2797151
OpenAlexW2158220148

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.