Evidence map›Paper›PMID 21949405›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Identification of the bacterial protein FtsX as a unique target of chemokine-mediated antimicrobial activity against Bacillus anthracis.

Matthew A Crawford, David E Lowe, Debra J Fisher, Scott Stibitz, Roger D Plaut, John W Beaber, Jason Zemansky, Borna Mehrad, Ian J Glomski, Robert M Strieter and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanistic insights into the regulation of cell wall hydrolysis by FtsEX and EnvC at the bacterial division site.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. G.I. pros: Antimicrobial defense in the gastrointestinal tract.Seminars in cell & developmental biology · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. Evolution of Antibiotic Resistance without Antibiotic Exposure.Antimicrobial agents and chemotherapy · 2017
    Article
  13. Frontiers in microbiology · 2017
    Article
  14. Article
  15. Article
  16. Chemokine-Derived Peptides: Novel Antimicrobial and Antineoplasic Agents.International journal of molecular sciences · 2015
    Review
  17. Review
  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 4 institutions in 1 country.

Matthew A CrawfordDepartment of Medicine, Division of Infectious Diseases, University of Virginia, Charlottesville, VA 22908, USA.
David E Lowe
Debra J Fisher
Scott Stibitz
Roger D Plaut
John W Beaber
Jason Zemansky
Borna Mehrad
Ian J Glomski
Robert M Strieter
Molly A Hughes
Office of Infectious Diseases · USCenter for Biologics Evaluation and Research · USUniversity of California, Berkeley · USUniversity of Virginia · US

Funding

INFECTIOUS DISEASES TRAINING PROGRAMT32AI007046 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Alison K Criss, William A Petri · 1985 to 2026
$15.3M
Global Biothreats Training ProgramT32AI055432 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI CRISS, ALISON K, PETRI, WILLIAM A · 2003 to 2022
$4.0M
Innate Immune Recognition of B. anthracisR21AI072469 · NIAID · UNIVERSITY OF VIRGINIA · PI HUGHES, MOLLY A · 2008 to 2009
$417k
NIAID NIH HHS R21 AI072469NIAID NIH HHS T32 AI007046NIAID NIH HHS T32 AI055432NIAID NIH HHS T32 AI055432-08
6 · The paper itself

Abstract

Chemokines are a family of chemotactic cytokines that function in host defense by orchestrating cellular movement during infection. In addition to this function, many chemokines have also been found to mediate the direct killing of a range of pathogenic microorganisms through an as-yet-undefined mechanism. As an understanding of the molecular mechanism and microbial targets of chemokine-mediated antimicrobial activity is likely to lead to the identification of unique, broad-spectrum therapeutic targets for effectively treating infection, we sought to investigate the mechanism by which the chemokine CXCL10 mediates bactericidal activity against the Gram-positive bacterium Bacillus anthracis, the causative agent of anthrax. Here, we report that disruption of the gene ftsX, which encodes the transmembrane domain of a putative ATP-binding cassette transporter, affords resistance to CXCL10-mediated antimicrobial effects against vegetative B. anthracis bacilli. Furthermore, we demonstrate that in the absence of FtsX, CXCL10 is unable to localize to its presumed site of action at the bacterial cell membrane, suggesting that chemokines interact with specific, identifiable bacterial components to mediate direct microbial killing. These findings provide unique insight into the mechanism of CXCL10-mediated bactericidal activity and establish, to our knowledge, the first description of a bacterial component critically involved in the ability of host chemokines to target and kill a bacterial pathogen. These observations also support the notion of chemokine-mediated antimicrobial activity as an important foundation for the development of innovative therapeutic strategies for treating infections caused by pathogenic, potentially multidrug-resistant microorganisms.

Indexed as

AnimalsAnti-Infective AgentsBacillus anthracisBacterial ProteinsCell Cycle ProteinsCell MembraneChemokine CXCL10Chemokine CXCL9Chemokines, CXCDrug Resistance, MicrobialGene DeletionGenes, BacterialGenetic Complementation TestHost-Pathogen InteractionsHumansMiceAnti-Infective AgentsBacterial ProteinsCell Cycle ProteinsChemokine CXCL10Chemokine CXCL9Chemokines, CXCCXCL10 protein, humanCxcl9 protein, mouseFtsX protein, bacteria

Identifiers

PMID21949405
PMCPMC3193227
OpenAlexW2054233737

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.