Evidence map›Paper›PMID 17301240›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Cleavage of p65/RelA of the NF-kappaB pathway by Chlamydia.

Sonya P Lad, Jiali Li, Jean da Silva Correia, Qilin Pan, Shilpa Gadwal, Richard J Ulevitch, Erguang Li

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
7.2field-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

51 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Tail-specific protease is an essentialInfection and immunity · 2024
    Article
  5. Article
  6. Review
  7. Review
  8. Frontiers in immunology · 2021
    Article
  9. Article
  10. Mutation of the Carboxy-Terminal Processing Protease inPathogens (Basel, Switzerland) · 2020
    Article
  11. The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019
    Review
  12. Clear Victory forFrontiers in microbiology · 2019
    Review
  13. Article
  14. Article
  15. Productive and Penicillin-StressedFrontiers in cellular and infection microbiology · 2017
    Article
  16. Review
  17. Production, crystallization and X-ray diffraction analysis of the protease CT441 from Chlamydia trachomatis.Acta crystallographica. Section F, Structural biology communications · 2015
    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

7 authors at 2 institutions in 2 countries.

Sonya P LadDepartment of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Jiali Li
Jean da Silva Correia
Qilin Pan
Shilpa Gadwal
Richard J Ulevitch
Erguang Li
Scripps Research Institute · USUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chlamydia trachomatis is a bacterial pathogen that infects the eyes and urogenital tract. Ocular infection by this organism is the leading cause of preventable blindness worldwide. The infection is also a leading cause of sexually transmitted disease in the United States. As obligate intracellular pathogens, chlamydiae have evolved sophisticated, yet undefined, mechanisms to maintain a favorable habitat for intracellular growth while avoiding harm to the host. We show here that chlamydiae have the ability to interfere with the NF-kappaB pathway of host inflammatory response. We found that Chlamydia infection did not promote IkappaBalpha degradation, a prerequisite for NF-kappaB nuclear translocation/activation, nor induce p65/RelA nuclear redistribution. Instead, it caused p65 cleavage into an N terminus-derived p40 fragment and a p22 of the C terminus. The activity was specific because no protein cleavage or degradation of NF-kappaB pathway components was detected. Moreover, murine p65 protein was resistant to cleavage by both human and mouse biovars. The chlamydial protein that selectively cleaved p65 was identified as a tail-specific protease (CT441). Importantly, expression of either this protease or the p40 cleavage product could block NF-kappaB activation. A hallmark of chlamydial STD is its asymptomatic nature, although inflammatory cellular response and chronic inflammation are among the underlying mechanisms. The data presented here demonstrate that chlamydiae have the ability to convert a regulatory molecule of host inflammatory response to a dominant negative inhibitor of the same pathway potentially to minimize inflammation.

Indexed as

AnimalsBacterial ProteinsChlamydia InfectionsChlamydia trachomatisHeLa CellsHumansI-kappa B ProteinsInclusion BodiesMiceNF-KappaB Inhibitor alphaNIH 3T3 CellsPeptide HydrolasesProtein Processing, Post-TranslationalSubstrate SpecificityTranscription Factor RelABacterial ProteinsI-kappa B ProteinsNF-KappaB Inhibitor alphaNFKBIA protein, humanNfkbia protein, mousePeptide HydrolasesTranscription Factor RelA

Identifiers

PMID17301240
PMCPMC1815284
OpenAlexW2094765978

What OpenQuestion holds

Textmetadata
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.