Evidence map›Paper›PMID 20510344›Full record

ArticleMicrobial pathogenesis2010

Autoprocessing and self-activation of the secreted protease CPAF in Chlamydia-infected cells.

Ding Chen, Lei Lei, Rhonda Flores, Zhiwei Huang, Zhongming Wu, Jijie Chai, Guangming Zhong

Open access · greenAbstract read
In one paragraph

Article in Microbial pathogenesis, 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
2.5field-weighted citation impact, top 13% 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, 25 citations in OpenAlex.

  1. Article
  2. Peptidase Inhibitor 15 (PI15) Regulates Chlamydial CPAF Activity.Frontiers in cellular and infection microbiology · 2018
    Article
  3. Chlamydial Plasmid-Dependent Pathogenicity.Trends in microbiology · 2017
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Cleavage of a putative metal permease in Chlamydia trachomatis yields an iron-dependent transcriptional repressor.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. Article
  15. 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

7 authors at 3 institutions in 3 countries.

Ding ChenDepartment of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
Lei Lei
Rhonda Flores
Zhiwei Huang
Zhongming Wu
Jijie Chai
Guangming Zhong
The University of Texas Health Science Center at San Antonio · USNational Institute of Biological Sciences, Beijing · CNBipar · FR

Funding

MECHANISMS OF CHLAMYDIAL EVASION OF IMMUNE RECOGNATIONR01AI047997 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI ZHONG, GUANGMING · 2000 to 2021
$6.9M
NIAID NIH HHS R01 AI047997
6 · The paper itself

Abstract

The Chlamydia-secreted protease/proteasome-like activity factor (CPAF) is synthesized as a proenzyme (proCPAF) and requires processing for proteolytic activity. Recent structural studies have further demonstrated that CPAF is a serine protease that can undergo autoprocessing and self-activation in a concentration-dependent manner in vitro. However, it is not known how CPAF is processed and activated during chlamydial infection. In the current study, we used a mutant CPAF designated as CPAF(E558A) that is deficient in processing by itself as a substrate to search for putative CPAF activation factor(s) in Chlamydia-infected cells. CPAF(E558A) was processed by the lysates made from Chlamydia-infected cells and the processing activity correlated with the presence of endogenous active CPAF in the fractionated lysate samples. CPAF produced in the Chlamydia-infected cells is required for processing the mutant CPAF(E558A) since the processing activity was removed by depletion with anti-CPAF but not control antibodies. Furthermore, a purified and activated wild type CPAF alone was sufficient for processing CPAF(E558A) and no other chlamydial proteases are required. Finally, fusion tag-induced oligomerization can lead to autoprocessing and self-activation of the wild type CPAF in mammalian cells. These observations together have demonstrated that CPAF undergoes autoprocessing and self-activation during chlamydial infection.

Indexed as

Amino Acid SubstitutionBacterial ProteinsChlamydia trachomatisHeLa CellsHumansMutant ProteinsMutation, MissenseSerine ProteasesVirulence FactorsBacterial ProteinsMutant ProteinsSerine ProteasesVirulence Factors

Identifiers

PMID20510344
PMCPMC2917482
OpenAlexW2039638264

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.