Evidence map›Paper›PMID 22714414›Full record

ArticleSmall GTPases

The taming of a Rab GTPase by Legionella pneumophila.

M Ramona Neunuebel, Matthias P Machner

Open access · hybridAbstract readComment
In one paragraph

Article in Small GTPases. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. AtypicalScience advances · 2022
    Article
  4. Article
  5. Article
  6. Review
  7. Structural and functional study of Legionella pneumophila effector RavA.Protein science : a publication of the Protein Society · 2021
    Article
  8. Review
  9. Frontiers in cellular and infection microbiology · 2020
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Inhibition of host cell translation elongation by Legionella pneumophila blocks the host cell unfolded protein response.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Maintenance of vacuole integrity by bacterial pathogens.Current opinion in microbiology · 2014
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

M Ramona NeunuebelCell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD USA.
Matthias P Machner
Eunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Virulence strategies of the respiratory pathogen Legionella pneumophilaZIAHD008893 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI MACHNER, MATTHIAS · 2010 to 2025
$19.6M
Intramural NIH HHS
6 · The paper itself

Abstract

Small GTPases of the Rab family represent an attractive target for microbial pathogens due to their role in controlling many aspects of intracellular cargo transport. Legionella pneumophila is an intravacuolar pathogen that survives inside host cells by manipulating protein trafficking pathways through a number of effector proteins secreted by the bacterium. These act as functional mimics of host proteins that modulate the activity of switch proteins such as guanosine triphosphatases (GTPases). L. pneumophila exploits the ER (endoplasmic reticulum)-to-Golgi vesicle transport pathway by modifying activity of Rab1, the GTPase regulating this pathway. This pathogen recruits Rab1 to the vacuole in which it resides, where effector proteins located on the surface of the vacuole regulate the activity status of Rab1 by mimicking the function of a guanine dissociation inhibitor (GDI) displacement factor, guanine exchange factor (GEF), or a GTPase-activating protein (GAP). In addition to these non-covalent modifications that alter the nucleotide binding state of Rab1, the bacterium also uses covalent modifications such as adenylylation (AMPylation) to control the dynamic of Rab1 on the Legionella-containing vacuole. Remarkably, AMPylation of Rab1 by SidM can be reversed by the L. pneumophila effector protein SidD, which exhibits de-AMPylation activity, demonstrating that L. pneumophila and related pathogens may utilize covalent modifications in order to transiently alter the activity of host proteins.

Indexed as

Adenosine MonophosphateAnimalsBacterial ProteinsHumansLegionella pneumophilarab1 GTP-Binding ProteinsVacuolesAdenosine MonophosphateBacterial Proteinsrab1 GTP-Binding Proteins

Identifiers

PMID22714414
PMCPMC3398914
OpenAlexW1969436275

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.