Evidence map›Paper›PMID 19801411›Full record

ArticleJournal of bacteriology2009

Cag3 is a novel essential component of the Helicobacter pylori Cag type IV secretion system outer membrane subcomplex.

Delia M Pinto-Santini, Nina R Salama

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. 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
4.7field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 45 citations in OpenAlex.

  1. Roles of the components of theFuture microbiology · 2024
    Review
  2. Distinct regions ofeLife · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Crystal structure of the type IV secretion system component CagX from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Assembly and mechanisms of bacterial type IV secretion machines.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  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

2 authors at 2 institutions in 1 country.

Delia M Pinto-SantiniDivision of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98109-1024, USA.
Nina R Salama
Fred Hutch Cancer Center · USUniversity of Washington · US

Funding

GENETIC REQUIREMENTS OF HELICOBACTER PYLORI INFECTIONR01AI054423 · NIAID · FRED HUTCHINSON CANCER RESEARCH CENTER · PI Nina Salama · 2004 to 2026
$9.5M
NIAID NIH HHS AI054423NIAID NIH HHS R01 AI054423
6 · The paper itself

Abstract

Helicobacter pylori strains harboring the cag pathogenicity island (PAI) have been associated with more severe gastric disease in infected humans. The cag PAI encodes a type IV secretion (T4S) system required for CagA translocation into host cells as well as induction of proinflammatory cytokines, such as interleukin-8 (IL-8). cag PAI genes sharing sequence similarity with T4S components from other bacteria are essential for Cag T4S function. Other cag PAI-encoded genes are also essential for Cag T4S, but lack of sequence-based or structural similarity with genes in existing databases has precluded a functional assignment for the encoded proteins. We have studied the role of one such protein, Cag3 (HP0522), in Cag T4S and determined Cag3 subcellular localization and protein interactions. Cag3 is membrane associated and copurifies with predicted inner and outer membrane Cag T4S components that are essential for Cag T4S as well as putative accessory factors. Coimmunoprecipitation and cross-linking experiments revealed specific interactions with HpVirB7 and CagM, suggesting Cag3 is a new component of the Cag T4S outer membrane subcomplex. Finally, lack of Cag3 lowers HpVirB7 steady-state levels, further indicating Cag3 makes a subcomplex with this protein.

Indexed as

Antigens, BacterialBacterial ProteinsCell Line, TumorChromatography, AffinityChromatography, GelGene Expression Regulation, BacterialHelicobacter InfectionsHelicobacter pyloriHumansImmunoprecipitationMass SpectrometryProtein BindingAntigens, BacterialBacterial Proteins

Identifiers

PMID19801411
PMCPMC2786551
OpenAlexW2033699453

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.