Evidence map›Paper›PMID 11698380›Full record

ArticleJournal of bacteriology2001

Isolation and characterization of Escherichia coli tolC mutants defective in secreting enzymatically active alpha-hemolysin.

H Vakharia, G J German, R Misra

Abstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Article
  2. Review
  3. Microorganisms · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Article
  16. Article
  17. Article
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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

3 authors.

H VakhariaDepartment of Microbiology, Arizona State University, Tempe, AZ 85287, USA.
G J German
R Misra

Funding

TARGETING AND ASSEMBLY OF E COLI OUTER MEMBRANE PROTEINSR01GM048167 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI MISRA, RAJEEV · 1997 to 2011
$2.4M
TARGETING &ASSEMBLY OF E COLI OUTER MEMBRANE PROTEINSR29GM048167 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI MISRA, RAJEEV · 1992 to 1996
–
NIGMS NIH HHS GM 48167NIGMS NIH HHS R01 GM048167
6 · The paper itself

Abstract

This study describes the isolation and characterization of a unique class of TolC mutants that, under steady-state growth conditions, secreted normal levels of largely inactive alpha-hemolysin. Unlike the reduced activity in the culture supernatants, the cell-associated hemolytic activity in these mutants was identical to that in the parental strain, thus reflecting a normal intracellular toxin activation event. Treatment of the secreted toxin with guanidine hydrochloride significantly restored cytolytic activity, suggesting that the diminished activity may have been due to the aggregation or misfolding of the toxin molecules. Consistent with this notion, sedimentation and filtration analyses showed that alpha-hemolysin secreted from the mutant strain has a mass greater than that secreted from the parental strain. Experiments designed to monitor the time course of alpha-hemolysin release showed delayed appearance of toxin in the culture supernatant of the mutant strain, thus indicating a possible defect in alpha-hemolysin translocation or release. Eight different TolC substitutions displaying this toxin secretion defect were scattered throughout the protein, of which six localized in the periplasmically exposed alpha-helical domain, while the remaining two mapped within the outer membrane-embedded beta-barrel domain of TolC. A plausible model for the secretion of inactive alpha-hemolysin in these TolC mutants is discussed in the context of the recently determined three-dimensional structure of TolC.

Indexed as

Escherichia coli ProteinsBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coliHemolysin ProteinsHemolysisMembrane Transport ProteinsMutationPhenotypeProtein ConformationBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coli ProteinsHemolysin ProteinsHlya protein, E coliMembrane Transport ProteinstolC protein, E coli

Identifiers

PMID11698380
PMCPMC95532

What OpenQuestion holds

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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.