Evidence map›Paper›PMID 23326233›Full record

ArticlePLoS pathogens2013

Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.

Rhys A Dunstan, Eva Heinz, Lakshmi C Wijeyewickrema, Robert N Pike, Anthony W Purcell, Timothy J Evans, Judyta Praszkier, Roy M Robins-Browne, Richard A Strugnell, Konstantin V Korotkov and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2013. 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
5.1field-weighted citation impact, top 4% 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, 61 citations in OpenAlex.

  1. Article
  2. Defining Membrane Protein Localization by Isopycnic Density Gradients.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
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  6. Forensic genomics of a novelMicrobial genomics · 2020
    Article
  7. Polymyxins Bind to the Cell Surface of UnculturableAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Article
  8. Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020
    Review
  9. Article
  10. Article
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  12. Review
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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

11 authors at 5 institutions in 2 countries.

Rhys A DunstanDepartment of Biochemistry and Molecular Biology, Monash University, Melbourne, Australia.
Eva Heinz
Lakshmi C Wijeyewickrema
Robert N Pike
Anthony W Purcell
Timothy J Evans
Judyta Praszkier
Roy M Robins-Browne
Richard A Strugnell
Konstantin V Korotkov
Trevor Lithgow
Monash University · AUUniversity of Kentucky · USUniversity of Melbourne · AUMelbourne Bioinformatics · AUMurdoch Children's Research Institute · AU

Funding

UNDERSTANDING THE MOLECULAR BASIS OF EPIGENETIC TRANSCRIPTIONAL SILENCINGP20RR020171 · NCRR · UNIVERSITY OF KENTUCKY · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 2004 to 2011
$16.5M
NCRR NIH HHS 2P20 RR020171NCRR NIH HHS P20 RR020171
6 · The paper itself

Abstract

The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBacterial Secretion SystemsBinding SitesComputational BiologyCrystallizationEvolution, MolecularGene Expression Regulation, BacterialKlebsiellaMolecular Sequence DataPhylogenyPorinsProtein BindingSecretinSpecies SpecificityVibrio choleraeBacterial Outer Membrane ProteinsBacterial Secretion SystemsPorinsPulS protein, Klebsiella oxytocaSecretin

Identifiers

PMID23326233
PMCPMC3542185
OpenAlexW2133790583

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.