Evidence map›Paper›PMID 24753609›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

An outer membrane channel protein of Mycobacterium tuberculosis with exotoxin activity.

Olga Danilchanka, Jim Sun, Mikhail Pavlenok, Christian Maueröder, Alexander Speer, Axel Siroy, Joeli Marrero, Carolina Trujillo, David L Mayhew, Kathryn S Doornbos and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

76 citing papers in PubMed, 131 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Secreted proteins ofFrontiers in tuberculosis · 2026
    Review
  6. Review
  7. Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026
    Review
  8. Review
  9. Article
  10. bioRxiv : the preprint server for biology · 2025
    Article
  11. Protease shaving ofMicrobiology spectrum · 2025
    Article
  12. TowardMicroorganisms · 2024
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. The C-terminus is essential for the stability of the mycobacterial channel protein MspA.Protein science : a publication of the Protein Society · 2024
    Article

16 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

15 authors at 3 institutions in 2 countries.

Olga DanilchankaDepartments of Microbiology and Radiation Oncology, University of Alabama at Birmingham, Birmingham, AL 35294.
Jim Sun
Mikhail Pavlenok
Christian Maueröder
Alexander Speer
Axel Siroy
Joeli Marrero
Carolina Trujillo
David L Mayhew
Kathryn S Doornbos
Luis E Muñoz
Martin Herrmann
Sabine Ehrt
Christian Berens
Michael Niederweis
Cornell University · USFriedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversity of Alabama at Birmingham · US

Funding

Target IdentificationP01AI074805 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2009 to 2013
$8.7M
Conditional Expression of Mycobacterial GenesR01AI063446 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI EHRT, SABINE · 2006 to 2022
$7.2M
Copper transport in Mycobacterium tuberculosisR01AI083632 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NIEDERWEIS, MICHAEL · 2009 to 2013
$1.8M
Porins of Mycobacterium tuberculosisR01AI063432 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NIEDERWEIS, MICHAEL · 2005 to 2009
$1.7M
NIAID NIH HHS AI063446NIAID NIH HHS AI074805NIAID NIH HHS AI083632NIAID NIH HHS AI63432NIAID NIH HHS P01 AI074805NIAID NIH HHS R01 AI063432NIAID NIH HHS R01 AI063446NIAID NIH HHS R01 AI083632
6 · The paper itself

Abstract

The ability to control the timing and mode of host cell death plays a pivotal role in microbial infections. Many bacteria use toxins to kill host cells and evade immune responses. Such toxins are unknown in Mycobacterium tuberculosis. Virulent M. tuberculosis strains induce necrotic cell death in macrophages by an obscure molecular mechanism. Here we show that the M. tuberculosis protein Rv3903c (channel protein with necrosis-inducing toxin, CpnT) consists of an N-terminal channel domain that is used for uptake of nutrients across the outer membrane and a secreted toxic C-terminal domain. Infection experiments revealed that CpnT is required for survival and cytotoxicity of M. tuberculosis in macrophages. Furthermore, we demonstrate that the C-terminal domain of CpnT causes necrotic cell death in eukaryotic cells. Thus, CpnT has a dual function in uptake of nutrients and induction of host cell death by M. tuberculosis.

Indexed as

Amino Acid SequenceAnimalsBacterial Outer Membrane ProteinsBacterial ToxinsCell LineExotoxinsGenes, BacterialGlycerolHEK293 CellsHumansJurkat CellsMacrophagesMiceMice, Inbred C57BLMolecular Sequence DataMutationBacterial Outer Membrane ProteinsBacterial ToxinsExotoxinsGlycerolRecombinant ProteinsRv3903 protein, Mycobacterium tuberculosisporesecretiontransport

Identifiers

PMID24753609
PMCPMC4020113
OpenAlexW2114020987

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.