ArticleBiochimie2010
A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin.
Article in Biochimie, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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.
Who cites it
6 citing papers in PubMed.
- Serine Protease Autotransporters of theMicroorganisms · 2019Review
- Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence.Cellular and molecular life sciences : CMLS · 2014Review
- Atypical enteropathogenic Escherichia coli secretes plasmid encoded toxin.BioMed research international · 2014Article
- VirK is a periplasmic protein required for efficient secretion of plasmid-encoded toxin from enteroaggregative Escherichia coli.Infection and immunity · 2012Article
- The autotransporter protein from Bordetella avium, Baa1, is involved in host cell attachment.Microbiological research · 2011Article
- Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae.Toxins · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Autotransporters are the most common virulence factors secreted from Gram-negative pathogens. Until recently, autotransporter folding and outer membrane translocation were thought to be self-mediated events that did not require accessory factors. Here, we report that two variants of the autotransporter plasmid-encoded toxin are secreted by a lab strain of Escherichia coli. Biophysical analysis and cell-based toxicity assays demonstrated that only one of the two variants was in a folded, active conformation. The misfolded variant was not produced by a pathogenic strain of enteroaggregative E. coli and did not result from protein overproduction in the lab strain of E. coli. Our data suggest a host-specific factor is required for efficient folding of plasmid-encoded toxin.
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Registered trials
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