Evidence map›Paper›PMID 22209629›Full record

ArticleChemistry & biology2012

ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein.

Jonathan P Renn, Mirco Junker, Richard N Besingi, Esther Braselmann, Patricia L Clark

Abstract read
In one paragraph

Article in Chemistry & biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Identification of an on-pathway intermediate illuminates the kinetic competition between protein folding and misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  7. Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Properties of protein unfolded states suggest broad selection for expanded conformational ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2019
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  15. Review
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  18. Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Protein science : a publication of the Protein Society · 2015
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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

5 authors at 1 institution in 1 country.

Jonathan P RennDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556-5670, USA.
Mirco Junker
Richard N Besingi
Esther Braselmann
Patricia L Clark
University of Notre Dame · US

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
OUTER MEMBRANE SECRETION MECHANISM FOR AUTOTRANSPORTER PROTEINSR01GM097573 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM097573NIGMS NIH HHS T32 GM075762
6 · The paper itself

Abstract

Autotransporter (AT) proteins are the largest class of extracellular virulence proteins secreted from Gram-negative bacteria. The mechanism by which AT proteins cross the bacterial outer membrane (OM), in the absence of ATP or another external energy source, is unknown. Here we demonstrate a linear correlation between localized regions of stability (ΔG(folding)) in the mature virulence protein (the AT "passenger") and OM secretion efficiency. Destabilizing the C-terminal β-helical domain of a passenger reduced secretion efficiency. In contrast, destabilizing the globular N-terminal domain of a passenger produced a linearly correlated increase in secretion efficiency. Thus, C-terminal passenger stability facilitates OM secretion, whereas N-terminal stability hinders it. The contributions of regional passenger stability to OM secretion demonstrate a crucial role for the passenger itself in directing its secretion, suggesting a novel type of ATP-independent, folding-driven transporter.

Indexed as

Adenosine TriphosphateBacterial Outer Membrane ProteinsBacterial ProteinsGram-Negative BacteriaModels, MolecularProtein FoldingProtein StabilityProtein Structure, TertiaryProtein TransportTetrahydrofolate DehydrogenaseVirulence Factors, BordetellaAdenosine TriphosphateBacterial Outer Membrane ProteinsBacterial ProteinspertactinTetrahydrofolate DehydrogenaseVirulence Factors, Bordetella

Identifiers

PMID22209629
PMCPMC3288764
OpenAlexW2029884778

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.