Evidence map›Paper›PMID 30250245›Full record

ArticleNature microbiology2018

Peptidoglycan editing by a specific LD-transpeptidase controls the muramidase-dependent secretion of typhoid toxin.

Tobias Geiger, Manuel Pazos, Maria Lara-Tejero, Waldemar Vollmer, Jorge E Galán

Open access · greenAbstract readLetter
In one paragraph

Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025
    Review
  4. Article
  5. Article
  6. iScience · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The diverse landscape of AB5-type toxins.Engineering microbiology · 2023
    Review
  16. Article
  17. Article
  18. Peptidoglycan deacetylation controls type IV secretion and the intracellular survival of the bacterial pathogenProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Tobias GeigerDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.ORCID http://orcid.org/0000-0002-8528-2849
Manuel PazosThe Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Maria Lara-TejeroDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.
Waldemar VollmerThe Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Jorge E GalánDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA. jorge.galan@yale.edu.ORCID http://orcid.org/0000-0002-6531-0355
Yale University · USNewcastle University · GB

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
Medical Research Council MR/N002679/1NIAID NIH HHS R01 AI079022NIAID NIH HHS R01 AI114618NIAID NIH HHS R56 AI079022
6 · The paper itself

Abstract

Protein secretion mechanisms are essential for the virulence of most bacterial pathogens. Typhoid toxin is an essential virulence factor for Salmonella Typhi, the cause of typhoid fever in humans. This toxin is unique in that it is only produced within mammalian cells, and it must be trafficked to the extracellular space before intoxicating target cells. An essential and poorly understood aspect of this transport pathway is the secretion of typhoid toxin from the bacterium into the S. Typhi-containing vacuole. We show here that typhoid toxin secretion requires its translocation to the trans side of the peptidoglycan layer at the bacterial poles for subsequent release through the outer membrane. This translocation process depends on a specialized muramidase, the activity of which requires the localized editing of peptidoglycan by a specific ld-transpeptidase. These studies describe a protein export mechanism that is probably conserved in other bacterial species.

Indexed as

Bacterial ProteinsBacterial ToxinsCell LineCell WallHumansMuramidasePeptidoglycanPeptidyl TransferasesProtein TransportSalmonella typhiTyphoid FeverVirulenceBacterial ProteinsBacterial ToxinsMuramidasePeptidoglycanPeptidyl Transferases

Identifiers

PMID30250245
PMCPMC7464686
OpenAlexW2890730734

What OpenQuestion holds

Textmetadata
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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.