Evidence map›Paper›PMID 30951565›Full record

ArticlePLoS pathogens2019

Unique features in the intracellular transport of typhoid toxin revealed by a genome-wide screen.

Shu-Jung Chang, Sheng Chih Jin, Xuyao Jiao, Jorge E Galán

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Protein-centric mechanisms of typhoidalFrontiers in cellular and infection microbiology · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. ThemBio · 2024
    Article
  9. Article
  10. Article
  11. The diverse landscape of AB5-type toxins.Engineering microbiology · 2023
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Bacterial AB toxins and host-microbe interactions.Advances in microbial physiology · 2022
    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

4 authors at 1 institution in 1 country.

Shu-Jung ChangDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, United States of America.
Sheng Chih JinDepartment of Genetics, Yale University School of Medicine, New Haven, Connecticut, United States of America.
Xuyao JiaoDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, United States of America.
Jorge E GalánDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, United States of America.ORCID 0000-0002-6531-0355
Yale University · US

Funding

Typhoid Toxin and Salmonella Typhi pathogenesisR01AI114618 · NIAID · YALE UNIVERSITY · PI GALAN, JORGE E · 2014 to 2023
$5.4M
Virulence factors of Salmonella TyphiR01AI079022 · NIAID · YALE UNIVERSITY · PI GALAN, JORGE E · 2008 to 2012
$2.0M
Virulence factors of Salmonella TyphiR56AI079022 · NIAID · YALE UNIVERSITY · PI GALAN, JORGE E · 2014 to 2014
$486k
NIAID NIH HHS R01 AI079022NIAID NIH HHS R01 AI114618NIAID NIH HHS R56 AI079022
6 · The paper itself

Abstract

Typhoid toxin is a virulence factor for Salmonella Typhi and Paratyphi, the cause of typhoid fever in humans. This toxin has a unique architecture in that its pentameric B subunit, made of PltB, is linked to two enzymatic A subunits, the ADP ribosyl transferase PltA and the deoxyribonuclease CdtB. Typhoid toxin is uniquely adapted to humans, recognizing surface glycoprotein sialoglycans terminated in acetyl neuraminic acid, which are preferentially expressed by human cells. The transport pathway to its cellular targets followed by typhoid toxin after receptor binding is currently unknown. Through a genome-wide CRISPR/Cas9-mediated screen we have characterized the mechanisms by which typhoid toxin is transported within human cells. We found that typhoid toxin hijacks specific elements of the retrograde transport and endoplasmic reticulum-associated degradation machineries to reach its subcellular destination within target cells. Our study reveals unique and common features in the transport mechanisms of bacterial toxins that could serve as the bases for the development of novel anti-toxin therapeutic strategies.

Indexed as

Endoplasmic Reticulum-Associated DegradationBacterial ProteinsBacterial ToxinsBiological TransportCRISPR-Cas SystemsHeLa CellsHumansIntracellular SpaceProtein BindingSalmonella typhiTyphoid FeverBacterial ProteinsBacterial Toxins

Identifiers

PMID30951565
PMCPMC6469816
OpenAlexW2928985712

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.