Evidence map›Paper›PMID 21883523›Full record

ArticleMolecular microbiology2011

Chlamydia trachomatis Slc1 is a type III secretion chaperone that enhances the translocation of its invasion effector substrate TARP.

Amanda J Brinkworth, Denise S Malcolm, António T Pedrosa, Katarzyna Roguska, Sevanna Shahbazian, James E Graham, Richard D Hayward, Rey A Carabeo

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.8field-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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Review
  3. mSphere · 2025
    Article
  4. Article
  5. Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023
    Review
  6. Frontiers in cellular and infection microbiology · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019
    Review
  11. Article
  12. The Loss of Expression of a Single Type 3 Effector (CT622) Strongly ReducesFrontiers in cellular and infection microbiology · 2018
    Article
  13. Article
  14. TheFrontiers in cellular and infection microbiology · 2017
    Article
  15. Review
  16. Article
  17. Article
  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

8 authors at 3 institutions in 2 countries.

Amanda J BrinkworthCentre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College, London SW72AZ, UK.
Denise S Malcolm
António T Pedrosa
Katarzyna Roguska
Sevanna Shahbazian
James E Graham
Richard D Hayward
Rey A Carabeo
Imperial College London · GBInstitute of Structural and Molecular Biology · GBUniversity of Louisville · US

Funding

CHLAMYDIAL INVASION OF NON-PHAGOCYTIC CELLSR01AI065545 · NIAID · WASHINGTON STATE UNIVERSITY · PI CARABEO, REY A · 2005 to 2021
$3.3M
Medical Research Council G0900213NIAID NIH HHS R01 AI065545
6 · The paper itself

Abstract

Bacterial type III secretion system (T3SS) chaperones pilot substrates to the export apparatus in a secretion-competent state, and are consequently central to the translocation of effectors into target cells. Chlamydia trachomatis is a genetically intractable obligate intracellular pathogen that utilizes T3SS effectors to trigger its entry into mammalian cells. The only well-characterized T3SS effector is TARP (translocated actin recruitment protein), but its chaperone is unknown. Here we exploited a known structural signature to screen for putative type III secretion chaperones encoded within the C. trachomatis genome. Using bacterial two-hybrid, co-precipitation, cross-linking and size exclusion chromatography we show that Slc1 (SycE-like chaperone 1; CT043) specifically interacts with a 200-amino-acid residue N-terminal region of TARP (TARP¹⁻²⁰⁰). Slc1 formed homodimers in vitro, as shown in cross-linking and gel filtration experiments. Biochemical analysis of an isolated Slc1-TARP¹⁻²⁰⁰ complex was consistent with a characteristic 2:1 chaperone-effector stoichiometry. Furthermore, Slc1 was co-immunoprecipitated with TARP from C. trachomatis elementary bodies. Also, coexpression of Slc1 specifically enhanced host cell translocation of TARP by a heterologous Yersinia enterocolitica T3SS. Taken together, we propose Slc1 as a chaperone of the C. trachomatis T3SS effector TARP.

Indexed as

Amino Acid MotifsAmino Acid SequenceBacterial ProteinsChlamydia InfectionsChlamydia trachomatisHeLa CellsHumansMolecular ChaperonesMolecular Sequence DataProtein BindingProtein TransportSequence AlignmentBacterial ProteinsMolecular Chaperones

Identifiers

PMID21883523
PMCPMC3214626
OpenAlexW1716361599

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.