Evidence map›Paper›PMID 20331642›Full record

ArticleCellular microbiology2010

Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule network.

Jeffrey Mital, Natalie J Miller, Elizabeth R Fischer, Ted Hackstadt

Open access · bronzeAbstract read
In one paragraph

Article in Cellular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed, 1 pooled it
7.6field-weighted citation impact, top 2% 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

88 citing papers in PubMed, 1 synthesis or guideline pooled it, 136 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Genome-wide association studies ofInfection and immunity · 2026
    Article
  4. Inclusion Membrane Proteins ofMicroorganisms · 2026
    Review
  5. Review
  6. mSphere · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023
    Review
  11. ThemBio · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Establishing the intracellular niche of obligate intracellular vacuolar pathogens.Frontiers in cellular and infection microbiology · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

28 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

4 authors at 2 institutions in 1 country.

Jeffrey MitalHost-Parasite Interactions Section, Laboratory of Intracellular Parasites, National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, MT 59840, USA.
Natalie J Miller
Elizabeth R Fischer
Ted Hackstadt
National Institute of Allergy and Infectious Diseases · USRocky Mountain Institute · US

Funding

Infectious Diseases Research Technologies Core - RMLZICAI001052 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CHERRY, JAMES · 2009 to 2025
$133.3M
Cellular Biology Of Host/parasite InteractionsZIAAI000567 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI HACKSTADT, TED · 2009 to 2025
$16.3M
Intramural NIH HHS Z99 AI999999Intramural NIH HHS ZIA AI000567
6 · The paper itself

Abstract

Chlamydiae are Gram-negative obligate intracellular bacteria that cause diseases with significant medical and economic impact. Chlamydia trachomatis replicates within a vacuole termed an inclusion, which is extensively modified by the insertion of a number of bacterial effector proteins known as inclusion membrane proteins (Incs). Once modified, the inclusion is trafficked in a dynein-dependent manner to the microtubule-organizing centre (MTOC), where it associates with host centrosomes. Here we describe a novel structure on the inclusion membrane comprised of both host and bacterial proteins. Members of the Src family of kinases are recruited to the chlamydial inclusion in an active form. These kinases display a distinct, localized punctate microdomain-like staining pattern on the inclusion membrane that colocalizes with four chlamydial inclusion membrane proteins (Incs) and is enriched in cholesterol. Biochemical studies show that at least two of these Incs stably interact with one another. Furthermore, host centrosomes associate with these microdomain proteins in C. trachomatis-infected cells and in uninfected cells exogenously expressing one of the chlamydial effectors. Together, the data suggest that a specific structure on the C. trachomatis inclusion membrane may be responsible for the known interactions of chlamydiae with the microtubule network and resultant effects on centrosome stability.

Indexed as

Bacterial ProteinsCentrosomeChlamydia InfectionsChlamydia trachomatisCytoplasmic DyneinsHeLa CellsHost-Pathogen InteractionsHumansInclusion BodiesMembrane MicrodomainsMembrane ProteinsMicrotubulesProtein Transportsrc-Family KinasesBacterial ProteinsCytoplasmic DyneinsMembrane Proteinssrc-Family Kinases

Identifiers

PMID20331642
PMCPMC2923664
OpenAlexW1567523745

What OpenQuestion holds

Textmetadata
LicenceTDM
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.