Evidence map›Paper›PMID 16291669›Full record

ArticleJournal of bacteriology2005

CheX is a phosphorylated CheY phosphatase essential for Borrelia burgdorferi chemotaxis.

M A Motaleb, Michael R Miller, Chunhao Li, Richard G Bakker, Stuart F Goldstein, Ruth E Silversmith, Robert B Bourret, Nyles W Charon

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.7field-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

45 citing papers in PubMed, 69 citations in OpenAlex.

  1. Distinct PlzC mechanisms integrate chemotaxis and c-di-GMP signaling to regulateProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Chemotaxis Coupling Protein CheWInfection and immunity · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Frontiers in immunology · 2017
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  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

8 authors at 3 institutions in 1 country.

M A MotalebDepartment of Microbiology, Immunology, and Cell Biology, Health Sciences Center, West Virginia University, Morgantown, 26506-9177, USA.
Michael R Miller
Chunhao Li
Richard G Bakker
Stuart F Goldstein
Ruth E Silversmith
Robert B Bourret
Nyles W Charon
University of North Carolina at Chapel Hill · USUniversity of Minnesota · USWest Virginia University · US

Funding

THE ROLE OF HEF1 PROTEIN IN INVASION OF METASTATIC BREAST CANCERP20RR016440 · NCRR · WEST VIRGINIA UNIVERSITY · PI GRABER, STEPHEN G · 2001 to 2010
$22.8M
Molecular Mechanisms of Signal Transduction by Two-Component Regulatory SystemsR01GM050860 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BOURRET, ROBERT B. · 1994 to 2025
$7.9M
BORRELIA BURGDORFERI MOTILITYR01AI029743 · NIAID · WEST VIRGINIA UNIVERSITY · PI CHARON, NYLES · 1990 to 2007
$2.1M
Role of motility in Borrelia burgdorferi pathogenesisR03AR050656 · NIAMS · WEST VIRGINIA UNIVERSITY · PI LI, CHUNHAO · 2004 to 2006
$223k
NCRR NIH HHS P20 RR016440NCRR NIH HHS RR16440NIAID NIH HHS AI29743NIAID NIH HHS R01 AI029743NIAMS NIH HHS R03 AR050656NIGMS NIH HHS GM 050860NIGMS NIH HHS R01 GM050860
6 · The paper itself

Abstract

Motility and chemotaxis are believed to be important in the pathogenesis of Lyme disease caused by the spirochete Borrelia burgdorferi. Controlling the phosphorylation state of CheY, a response regulator protein, is essential for regulating bacterial chemotaxis and motility. Rapid dephosphorylation of phosphorylated CheY (CheY-P) is crucial for cells to respond to environmental changes. CheY-P dephosphorylation is accomplished by one or more phosphatases in different species, including CheZ, CheC, CheX, FliY, and/or FliY/N. Only a cheX phosphatase homolog has been identified in the B. burgdorferi genome. However, a role for cheX in chemotaxis has not been established in any bacterial species. Inactivating B. burgdorferi cheX by inserting a flgB-kan cassette resulted in cells (cheX mutant cells) with a distinct motility phenotype. While wild-type cells ran, paused (stopped or flexed), and reversed, the cheX mutant cells continuously flexed and were not able to run or reverse. Furthermore, swarm plate and capillary tube chemotaxis assays demonstrated that cheX mutant cells were deficient in chemotaxis. Wild-type chemotaxis and motility were restored when cheX mutant cells were complemented with a shuttle vector expressing CheX. Furthermore, CheX dephosphorylated CheY3-P in vitro and eluted as a homodimer in gel filtration chromatography. These findings demonstrated that B. burgdorferi CheX is a CheY-P phosphatase that is essential for chemotaxis and motility, which is consistent with CheX being the only CheY-P phosphatase in the B. burgdorferi chemotaxis signal transduction pathway.

Indexed as

Signal TransductionBacterial ProteinsBorrelia burgdorferiChemotaxisLocomotionMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMutationPhosphoric Monoester HydrolasesPhosphorylationBacterial ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsPhosphoric Monoester Hydrolases

Identifiers

PMID16291669
PMCPMC1291287
OpenAlexW2143452674

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.