Evidence map›Paper›PMID 20096108›Full record

ArticleBMC microbiology2010

Interactions between flagellar and type III secretion proteins in Chlamydia pneumoniae.

Chris B Stone, David C Bulir, Jodi D Gilchrist, Raman K Toor, James B Mahony

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023
    Review
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  6. Review
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  15. Unity in variety--the pan-genome of the Chlamydiae.Molecular biology and evolution · 2011
    Article
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

Chris B StoneM,G, DeGroote Institute for Infectious Disease Research, Faculty of Health Sciences and the Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Ontario, Canada.
David C Bulir
Jodi D Gilchrist
Raman K Toor
James B Mahony
McMaster University · CASt. Joseph’s Healthcare Hamilton · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

backgroundFlagellar secretion systems are utilized by a wide variety of bacteria to construct the flagellum, a conserved apparatus that allows for migration towards non-hostile, nutrient rich environments. Chlamydia pneumoniae is an obligate, intracellular pathogen whose genome contains at least three orthologs of flagellar proteins, namely FliI, FlhA and FliF, but the role of these proteins remains unknown.

resultsFull length FliI, and fragments of FlhA, FliF, and FliI, were cloned and expressed as either GST or His tagged proteins in E. coli. The GST-tagged full length FliI protein was shown to possess ATPase activity, hydrolyzing ATP at a rate of 0.15 +/- .02 micromol min-1 mg-1 in a time- and dose-dependant manner. Using bacterial-2-hybrid and GST pull-down assays, the N-terminal domain of FliI was shown to interact with the cytoplasmic domain of FlhA, but not with FliF, and the cytoplasmic domain of FlhA was shown to interact with the C-terminus of FliF. The absence of other flagellar orthologs led us to explore cross-reaction of flagellar proteins with type III secretion proteins, and we found that FliI interacted with CdsL and CopN, while FlhA interacted with CdsL and Cpn0322 (YscU ortholog CdsU).

conclusionsThe specific interaction of the four orthologous flagellar proteins in C. pneumoniae suggests that they interact in vivo and, taken together with their conservation across members of the chlamydiae sps., and their interaction with T3S components, suggests a role in bacterial replication and/or intracellular survival.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsChlamydophila pneumoniaeGlutathioneMembrane ProteinsMolecular Sequence DataRecombinant Fusion ProteinsSequence AlignmentSequence Analysis, DNATwo-Hybrid System TechniquesAdenosine TriphosphatasesBacterial ProteinsFlhA protein, BacteriaFlif protein, BacteriaFliL protein, BacteriaGlutathioneMembrane ProteinsRecombinant Fusion Proteins

Identifiers

PMID20096108
PMCPMC2830194
OpenAlexW2011559993

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.