Evidence map›Paper›PMID 26185092›Full record

ReviewMicrobiology spectrum2015

Multifunctional-autoprocessing repeats-in-toxin (MARTX) Toxins of Vibrios.

Karla J F Satchell

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology spectrum, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
8.0field-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

71 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025
    Article
  9. Enigmatic roles ofJournal of bacteriology · 2025
    Review
  10. Article
  11. Science advances · 2025
    Article
  12. Effects of vitamin BApplied and environmental microbiology · 2025
    Article
  13. Article
  14. Non-toxigenicArchive of clinical cases · 2025
    Review
  15. Article
  16. Article
  17. Biantennary N-glycans As Receptors for MARTX Toxins inbioRxiv : the preprint server for biology · 2024
    Article
  18. Antagonistic effects of actin-specific toxins onbioRxiv : the preprint server for biology · 2024
    Article
  19. Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Non-O1/Non-O139Microorganisms · 2024
    Review

11 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Karla J F SatchellDepartment of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611.
Northwestern University · US

Funding

Molecular mechanism of V. vulnificus MARTX toxin in pathogenesis and food safetyR01AI092825 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SATCHELL, KARLA J F · 2011 to 2021
$4.1M
Vibrio MARTX toxin effectors in signaling and pathogenesisR37AI092825 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Karla J F Satchell · 2022 to 2026
$2.5M
Function of Vibrio vulnificus MARTX toxin during early gut infectionR01AI098369 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SATCHELL, KARLA J F · 2012 to 2016
$1.3M
NIAID NIH HHS R01 AI092825NIAID NIH HHS R01 AI098369NIAID NIH HHS R37 AI092825
6 · The paper itself

Abstract

Multifunctional-autoprocessing repeats-in-toxin (MARTX) toxins are a heterogeneous group of toxins found in a number of Vibrio species and other Gram-negative bacteria. The toxins are composed of conserved repeat regions and an autoprocessing protease domain that together function as a delivery platform for transfer of cytotoxic and cytopathic domains into target eukaryotic cell cytosol. Within the cells, the effectors can alter biological processes such as signaling or cytoskeletal structure, presumably to the benefit of the bacterium. Ten effector domains are found in the various Vibrio MARTX toxins, although any one toxin carries only two to five effector domains. The specific toxin variant expressed by a species can be modified by homologous recombination to acquire or lose effector domains, such that different strains within the same species can express distinct variants of the toxins. This review examines the conserved structural elements of the MARTX toxins and details the different toxin arrangements carried by Vibrio species and strains. The catalytic function of domains and how the toxins are linked to pathogenesis of human and animals is described.

Indexed as

Bacterial ToxinsHumansProtein Structure, TertiaryProtein TransportSeafoodType III Secretion SystemsType IV Secretion SystemsVibrioVibrio InfectionsBacterial ToxinsRtxA protein, Vibrio choleraeType III Secretion SystemsType IV Secretion Systems

Identifiers

PMID26185092
PMCPMC4509488
OpenAlexW2415437789

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.