Evidence map›Paper›PMID 22711538›Full record

ArticleThe Journal of biological chemistry2012

Domain analyses reveal that Chlamydia trachomatis CT694 protein belongs to the membrane-localized family of type III effector proteins.

Holly D Bullock, Suzanne Hower, Kenneth A Fields

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Article
  2. Review
  3. The serodiagnositic value ofFrontiers in public health · 2024
    Article
  4. Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023
    Review
  5. Molecular pathogenesis ofFrontiers in cellular and infection microbiology · 2023
    Review
  6. Frontiers in cellular and infection microbiology · 2023
    Article
  7. Review
  8. Article
  9. Chlamydia-induced curvature of the host-cell plasma membrane is required for infection.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Chlamydia cell biology and pathogenesis.Nature reviews. Microbiology · 2016
    Review
  18. Article
  19. Article
  20. Conserved type III secretion system exerts important roles in Chlamydia trachomatis.International journal of clinical and experimental pathology · 2014
    Review
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

3 authors.

Holly D BullockDepartment of Microbiology and Immunology, The Miller School of Medicine, Miami, Florida 33136, USA.
Suzanne Hower
Kenneth A Fields

Funding

Type III exported effectors of Chlamydia trachomatisR01AI065530 · NIAID · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI FIELDS, KENNETH A · 2005 to 2021
$5.7M
NIAID NIH HHS AI065530NIAID NIH HHS R01 AI065530
6 · The paper itself

Abstract

The Chlamydia trachomatis type three-secreted effector protein CT694 is expressed during late-cycle development yet is secreted by infectious particles during the invasion process. We have previously described the presence of at least two functional domains within CT694. CT694 was found to interact with the human protein Ahnak through a C-terminal domain and affect formation of host-cell actin stress fibers. Immunolocalization analyses of ectopically expressed pEGFP-CT694 also revealed plasma membrane localization for CT694 that was independent of Ahnak binding. Here we provide evidence that CT694 contains multiple functional domains. Plasma membrane localization and CT694-induced alterations in host cell morphology are dependent on an N-terminal domain. We demonstrate that membrane association of CT694 is dependent on a domain resembling a membrane localization domain (MLD) found in anti-host proteins from Yersinia, Pseudomonas, and Salmonella spp. This domain is necessary and sufficient for localization and morphology changes but is not required for Ahnak binding. Further, the CT694 MLD is able to complement ExoS ΔMLD when ectopically expressed. Taken together, our data indicate that CT694 is a multidomain protein with the potential to modulate multiple host cell processes.

Indexed as

Bacterial ProteinsCell MembraneChlamydia InfectionsChlamydia trachomatisHeLa CellsHumansMembrane ProteinsNeoplasm ProteinsProtein Structure, TertiaryPseudomonasSalmonellaStress FibersYersiniaAHNAK protein, humanBacterial ProteinsMembrane ProteinsNeoplasm Proteins

Identifiers

PMID22711538
PMCPMC3431695

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Registered trials

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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.