Evidence map›Paper›PMID 23852872›Full record

ArticleJournal of bacteriology2013

Mutations in hemG mediate resistance to salicylidene acylhydrazides, demonstrating a novel link between protoporphyrinogen oxidase (HemG) and Chlamydia trachomatis infectivity.

Patrik Engström, Bidong D Nguyen, Johan Normark, Ingela Nilsson, Robert J Bastidas, Asa Gylfe, Mikael Elofsson, Kenneth A Fields, Raphael H Valdivia, Hans Wolf-Watz and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023
    Review
  4. Article
  5. The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019
    Review
  6. Review
  7. Article
  8. Article
  9. The Loss of Expression of a Single Type 3 Effector (CT622) Strongly ReducesFrontiers in cellular and infection microbiology · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  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

11 authors at 3 institutions in 2 countries.

Patrik EngströmDepartment of Molecular Biology, Laboratory for Molecular Infection Medicine, Sweden.
Bidong D Nguyen
Johan Normark
Ingela Nilsson
Robert J Bastidas
Asa Gylfe
Mikael Elofsson
Kenneth A Fields
Raphael H Valdivia
Hans Wolf-Watz
Sven Bergström
Umeå University · SEDuke University · USUniversity of Miami · US

Funding

Type III exported effectors of Chlamydia trachomatisR01AI065530 · NIAID · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI FIELDS, KENNETH A · 2005 to 2021
$5.7M
Forward and Reverse Genetics in ChlamydiaR01AI100759 · NIAID · DUKE UNIVERSITY · PI VALDIVIA, RAPHAEL H · 2012 to 2016
$2.2M
Chlamydia Effector ProteinsR01AI081694 · NIAID · DUKE UNIVERSITY · PI VALDIVIA, RAPHAEL H · 2010 to 2014
$1.9M
NIAID NIH HHS AI065530NIAID NIH HHS AI081694NIAID NIH HHS AI100759NIAID NIH HHS R01 AI065530NIAID NIH HHS R01 AI081694NIAID NIH HHS R01 AI100759
6 · The paper itself

Abstract

Salicylidene acylhydrazides (SAHs) inhibit the type III secretion system (T3S) of Yersinia and other Gram-negative bacteria. In addition, SAHs restrict the growth and development of Chlamydia species. However, since the inhibition of Chlamydia growth by SAH is suppressed by the addition of excess iron and since SAHs have an iron-chelating capacity, their role as specific T3S inhibitors is unclear. We investigated here whether SAHs exhibit a function on C. trachomatis that goes beyond iron chelation. We found that the iron-saturated SAH INP0341 (IS-INP0341) specifically affects C. trachomatis infectivity with reduced generation of infectious elementary body (EB) progeny. Selection and isolation of spontaneous SAH-resistant mutant strains revealed that mutations in hemG suppressed the reduced infectivity caused by IS-INP0341 treatment. Structural modeling of C. trachomatis HemG predicts that the acquired mutations are located in the active site of the enzyme, suggesting that IS-INP0341 inhibits this domain of HemG and that protoporphyrinogen oxidase (HemG) and heme metabolism are important for C. trachomatis infectivity.

Indexed as

MutationAmino Acid SequenceBacterial ProteinsCatalytic DomainChlamydia trachomatisDrug Resistance, BacterialHeLa CellsHemeHumansHydrazinesIronModels, MolecularMolecular Sequence DataProtoporphyrinogen OxidaseBacterial ProteinsHemeHydrazinesINP 0341IronProtoporphyrinogen Oxidase

Identifiers

PMID23852872
PMCPMC3754756
OpenAlexW2013799812

What OpenQuestion holds

Textmetadata
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.