Evidence map›Paper›PMID 26780191›Full record

ArticleCellular microbiology2016

MARTX effector cross kingdom activation by Golgi-associated ADP-ribosylation factors.

Byoung Sik Kim, Karla J F Satchell

Open access · greenAbstract read
In one paragraph

Article in Cellular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 18 citations in OpenAlex.

  1. Pathogen hijacks focal adhesion signaling by a T3SS effector CteX.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Cross-Kingdom Activation ofJournal of bacteriology · 2020
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. 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

2 authors at 1 institution in 1 country.

Byoung Sik KimDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL, 60611, USA.
Karla J F SatchellDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL, 60611, USA.
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

Vibrio vulnificus infects humans and causes lethal septicemia. The primary virulence factor is a multifunctional-autoprocessing repeats-in-toxin (MARTX) toxin consisting of conserved repeats-containing regions and various effector domains. Recent genomic analyses for the newly emerged V. vulnificus biotype 3 strain revealed that its MARTX toxin has two previously unknown effector domains. Herein, we characterized one of these domains, Domain X (DmXVv ). A structure-based homology search revealed that DmXVv belongs to the C58B cysteine peptidase subfamily. When ectopically expressed in cells, DmXVv was autoprocessed and induced cytopathicity including Golgi dispersion. When the catalytic cysteine or the region flanking the scissile bond was mutated, both autoprocessing and cytopathicity were significantly reduced indicating that DmXVv cytopathicity is activated by amino-terminal autoprocessing. Consistent with this, host cell protein export was affected by Vibrio cells producing a toxin with wild-type, but not catalytically inactive, DmXVv . DmXVv was found to localize to Golgi and to directly interact with Golgi-associated ADP-ribosylation factors ARF1, ARF3 and ARF4, although ARF binding was not necessary for the subcellular localization. Rather, this interaction was found to induce autoprocessing of DmXVv . These data demonstrate that the V. vulnificus hijacks the host ARF proteins to activate the cytopathic DmXVv effector domain of MARTX toxin.

Indexed as

ADP-Ribosylation FactorsAmino Acid SequenceBacterial ToxinsGolgi ApparatusHEK293 CellsHeLa CellsHost-Pathogen InteractionsHumansPhenotypeProtein TransportVibrio InfectionsVibrio vulnificusVirulence FactorsADP-Ribosylation FactorsBacterial ToxinsVirulence Factors

Identifiers

PMID26780191
PMCPMC5016026
OpenAlexW2294637065

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.