Evidence map›Paper›PMID 24573681›Full record

ArticleThe Journal of biological chemistry2014

Bacillus cereus Certhrax ADP-ribosylates vinculin to disrupt focal adhesion complexes and cell adhesion.

Nathan C Simon, Joseph T Barbieri

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  3. Review
  4. You Can'tFrontiers in microbiology · 2020
    Review
  5. Article
  6. TheMicrobiology spectrum · 2019
    Review
  7. Article
  8. Review
  9. 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

2 authors at 1 institution in 1 country.

Nathan C SimonDepartment of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226.
Joseph T BarbieriDepartment of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226. Electronic address: jtb01@mcw.edu.
Medical College of Wisconsin · US

Funding

Vaccines and Therapies Against BotulismU54AI057153 · NIAID · UNIVERSITY OF CHICAGO · PI SHUMAN, HOWARD A · 2003 to 2013
$87.6M
Mechanisms of Bacterial Toxin ActionR01AI030162 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI BARBIERI, JOSEPH T · 1990 to 2019
$6.7M
ENDOSTEAL BONE VOLUME REGULATION AND OSTEOPOROSISR01AR031062 · NIAMS · LOMA LINDA VETERANS ASSN RESEARCH &EDUC · PI MOHAN, SUBBURAMAN · 1986 to 2014
$3.5M
Contribution of Certhrax to Virulence of Anthrax-like Bacillus cereus StrainR21AI111101 · NIAID · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI BARBIERI, JOSEPH T, O'BRIEN, ALISON DAVIS · 2015 to 2016
$428k
NIAID NIH HHS R01 AI030162NIAID NIH HHS R01 AI031062NIAID NIH HHS R21 AI111101NIAID NIH HHS U54 AI057153NIAMS NIH HHS R01 AR031062
6 · The paper itself

Abstract

Bacillus cereus is often associated with mild to moderate gastroenteritis; however, some recent isolates cause inhalational anthrax-like diseases and death. These potential emerging human pathogens express multiple virulence factors. B. cereus strain G9241 expresses anthrax toxin, several polysaccharide capsules, and the novel ADP-ribosyltransferase, Certhrax. In this study, we show that Certhrax ADP-ribosylates Arg-433 of vinculin, a protein that coordinates actin cytoskeleton and extracellular matrix interactions. ADP-ribosylation of vinculin disrupted focal adhesion complexes and redistributed vinculin to the cytoplasm. Exogenous vinculin rescued these phenotypes. This provides a mechanism for strain G9241 to breach host barrier defenses and promote bacterial growth and spread. Certhrax is the first bacterial toxin to add a post-translational modification to vinculin to disrupt the actin cytoskeleton.

Indexed as

ActinsAdenosine Diphosphate RiboseADP Ribose TransferasesAmino Acid SequenceAntigens, BacterialBacillus cereusBacterial ProteinsBacterial ToxinsCell AdhesionCytoskeletonExtracellular MatrixFocal AdhesionsHeLa CellsHumansImmunity, InnateMolecular Sequence DataActinsAdenosine Diphosphate RiboseADP Ribose Transferasesanthrax toxinAntigens, BacterialBacterial ProteinsBacterial Toxinscerthrax toxin, Bacillus cereusRecombinant ProteinsStreptavidinVinculinActinADP-ribosylationBacillusBacterial ToxinsMicroscopic Imaging

Identifiers

PMID24573681
PMCPMC4036183
OpenAlexW2094496775

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.