Evidence map›Paper›PMID 23469034›Full record

ArticlePloS one2013

Delivery of CdiA nuclease toxins into target cells during contact-dependent growth inhibition.

Julia S Webb, Kiel C Nikolakakis, Julia L E Willett, Stephanie K Aoki, Christopher S Hayes, David A Low

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Antimicrobial Weapons of Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022
    Article
  7. The Type VII Secretion System ofAnnual review of microbiology · 2021
    Article
  8. Microbial genomics · 2021
    Article
  9. Article
  10. Contact-Dependent Growth Inhibition in Bacteria: Do Not Get Too Close!International journal of molecular sciences · 2020
    Review
  11. A membrane-depolarizing toxin substrate of theProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Capsule ProtectsFrontiers in microbiology · 2020
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

6 authors at 1 institution in 1 country.

Julia S WebbDepartment of Molecular, Cellular and Developmental Biology, University of California Santa Barbara, Santa Barbara, California, United States of America.
Kiel C Nikolakakis
Julia L E Willett
Stephanie K Aoki
Christopher S Hayes
David A Low
University of California, Santa Barbara · US

Funding

Vaccines and Diagnostics TrialsU54AI065359 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI BARBOUR, ALAN G. · 2005 to 2013
$88.8M
Molecular determinants of A-site mRNA cleavage ribosomeR01GM078634 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI HAYES, CHRISTOPHER S. · 2006 to 2014
$2.5M
NIAID NIH HHS U54 AI065359NIAID NIH HHS U54AI065359NIGMS NIH HHS GM078634NIGMS NIH HHS R01 GM078634
6 · The paper itself

Abstract

Bacterial contact-dependent growth inhibition (CDI) is mediated by the CdiB/CdiA family of two-partner secretion proteins. CDI systems deploy a variety of distinct toxins, which are contained within the polymorphic C-terminal region (CdiA-CT) of CdiA proteins. Several CdiA-CTs are nucleases, suggesting that the toxins are transported into the target cell cytoplasm to interact with their substrates. To analyze CdiA transfer to target bacteria, we used the CDI system of uropathogenic Escherichia coli 536 (UPEC536) as a model. Antibodies recognizing the amino- and carboxyl-termini of CdiA(UPEC536) were used to visualize transfer of CdiA from CDI(UPEC536+) inhibitor cells to target cells using fluorescence microscopy. The results indicate that the entire CdiA(UPEC536) protein is deposited onto the surface of target bacteria. CdiA(UPEC536) transfer to bamA101 mutants is reduced, consistent with low expression of the CDI receptor BamA on these cells. Notably, our results indicate that the C-terminal CdiA-CT toxin region of CdiA(UPEC536) is translocated into target cells, but the N-terminal region remains at the cell surface based on protease sensitivity. These results suggest that the CdiA-CT toxin domain is cleaved from CdiA(UPEC536) prior to translocation. Delivery of a heterologous Dickeya dadantii CdiA-CT toxin, which has DNase activity, was also visualized. Following incubation with CDI(+) inhibitor cells targets became anucleate, showing that the D.dadantii CdiA-CT was delivered intracellularly. Together, these results demonstrate that diverse CDI toxins are efficiently translocated across target cell envelopes.

Indexed as

Bacterial Outer Membrane ProteinsCoculture TechniquesCytoplasmEscherichia coliEscherichia coli ProteinsMembrane ProteinsMolecular ImagingProtein TransportBacterial Outer Membrane ProteinsBamA protein, E coliCdiA protein, E coliEscherichia coli ProteinsMembrane Proteins

Identifiers

PMID23469034
PMCPMC3585180
OpenAlexW2017187178

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.