Evidence map›Paper›PMID 24118465›Full record

ArticleMolecular microbiology2013

An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core.

Richard N Besingi, Julie L Chaney, Patricia L Clark

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
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

3 authors at 1 institution in 1 country.

Richard N BesingiDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Julie L Chaney
Patricia L Clark
University of Notre Dame · US

Funding

OUTER MEMBRANE SECRETION MECHANISM FOR AUTOTRANSPORTER PROTEINSR01GM097573 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2011 to 2014
$1.1M
NIGMS NIH HHS 1R01 GM097573NIGMS NIH HHS R01 GM097573
6 · The paper itself

Abstract

Autotransporter (AT) proteins are a broad class of virulence factors from Gram-negative pathogens. AT outer membrane (OM) secretion appears simple in many regards, yet the mechanism that enables transport of the central AT 'passenger' across the OM remains unclear. OM secretion efficiency for two AT passengers is enhanced by approximately 20 kDa stable core at the C-terminus of the passenger, but studies on a broader range of AT proteins are needed in order to determine whether a stability difference between the passenger N- and C-terminus represents a truly common mechanistic feature. Yersinia pestis YapV is homologous to Shigella flexneri IcsA, and like IcsA, YapV recruits mammalian neural Wiskott-Aldrich syndrome protein (N-WASP). In vitro, the purified YapV passenger is functional and rich in β-sheet structure, but lacks a approximately 20 kDa C-terminal stable core. However, the N-terminal 49 residues of the YapV passenger globally destabilize the entire YapV passenger, enhancing its OM secretion efficiency. These results indicate that the contributions of AT passenger sequences to OM secretion efficiency extend beyond a C-terminal stable core, and highlight a role of the passenger N-terminus in reducing passenger stability in order to facilitate OM secretion of some AT proteins.

Indexed as

Bacterial Secretion SystemsAmino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsCircular DichroismMembrane Transport ProteinsModels, MolecularProtein ConformationProtein FoldingProtein StabilityProtein Structure, SecondarySequence Homology, Amino AcidWiskott-Aldrich Syndrome ProteinYersinia pestisBacterial Outer Membrane ProteinsBacterial ProteinsBacterial Secretion SystemsMembrane Transport ProteinsWiskott-Aldrich Syndrome Protein

Identifiers

PMID24118465
PMCPMC3857143
OpenAlexW1904809137

What OpenQuestion holds

Textmetadata
LicenceTDM
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.