Evidence map›Paper›PMID 16954394›Full record

ArticleInfection and immunity2006

Protease activity, secretion, cell entry, cytotoxicity, and cellular targets of secreted autotransporter toxin of uropathogenic Escherichia coli.

Nathalie M Maroncle, Kelsey E Sivick, Rebecca Brady, Faye-Ellen Stokes, Harry L T Mobley

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

34 citing papers in PubMed, 61 citations in OpenAlex.

  1. The Role ofInternational journal of molecular sciences · 2025
    Review
  2. Plasmid-encoded toxin ofFrontiers in cellular and infection microbiology · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Extraintestinal PathogenicPathogens (Basel, Switzerland) · 2021
    Review
  7. Article
  8. Article
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  10. Review
  11. Review
  12. 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

5 authors at 3 institutions in 2 countries.

Nathalie M MaroncleDepartment of Microbiology and Immunology, University of Michigan Medical School, 5641 Medical Science Bldg II, 1150 West Medical Center Dr., Ann Arbor, MI 48109-0620, USA.
Kelsey E Sivick
Rebecca Brady
Faye-Ellen Stokes
Harry L T Mobley
University of Michigan–Ann Arbor · USMicrobiology Society · GBUniversity of Maryland, Baltimore · US

Funding

MOLECULAR PATHOGENESIS OF E COLI UTIR01AI043363 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MOBLEY, HARRY L. · 1998 to 2012
$3.4M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
Vaccine to prevent E. coli urinary tract infectionR56AI043363 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MOBLEY, HARRY L. · 2014 to 2014
$351k
NIAID NIH HHS AI43363NIAID NIH HHS R01 AI043363NIAID NIH HHS R56 AI043363NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

The secreted autotransporter toxin (Sat), found predominantly in uropathogenic Escherichia coli, is a member of the SPATE (serine protease autotransporters of Enterobacteriaceae) family and, as such, has serine protease activity and causes cytopathic effects on various cell types. To assess the contribution of the serine protease active site to the mechanism of action of Sat, mutations were made in the first (S256I), in the second (S258A), or in both (S256I/S258A) serine residues within the active site motif. Mutations in the first or both serines reduced protease activity to background levels (P<0.001); a single mutation in the second serine reduced activity by 60% compared to wild type (P<0.001). After reversion of the S256I mutation to wild type (I256S), we confirmed S256 as the catalytically active serine. None of these mutations affected secretion of the mature passenger domain or release into the supernatant. The S256I mutation, however, abrogated the cytotoxicity of Sat on human bladder (UM-UC-3) and kidney (HEK 293) epithelial cells, characterized by rounding and elongation, respectively, and a high level of cell detachment. Moreover, S256 is essential for Sat to mediate cytoskeletal contraction and actin loss in host cells as well as to degrade specific membrane/cytoskeletal (fodrin and leukocyte function-associated molecule 1) and nuclear [microtubule-associated proteins, LIM domain-only protein 7, Rap GTPase-activating protein, poly(ADP-ribose) polymerase] proteins in vitro. Lastly, Sat was internalized by host cells and localized to the cytoskeletal fraction where membrane/cytoskeletal target proteins reside.

Indexed as

Bacterial ToxinsCell LineCells, CulturedEscherichia coliEscherichia coli InfectionsEscherichia coli ProteinsHumansKidneyMutagenesis, Site-DirectedSerine EndopeptidasesUrinary BladderUrotheliumBacterial ToxinsEscherichia coli Proteinssecreted autotransporter toxin, E coliSerine Endopeptidases

Identifiers

PMID16954394
PMCPMC1695523
OpenAlexW2111069670

What OpenQuestion holds

Textmetadata
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.