Evidence map›Paper›PMID 31974499›Full record

ArticleScientific reports2020

An intra-bacterial activity for a T3SS effector.

Samir El Qaidi, Nichollas E Scott, Michael P Hays, Brian V Geisbrecht, Shelby Watkins, Philip R Hardwidge

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. 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
3.9field-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

25 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The T3SS Effector Protease NleC Is Active withinPathogens (Basel, Switzerland) · 2021
    Article
  17. Article
  18. Article
  19. Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021
    Review
  20. Review
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

6 authors at 2 institutions in 2 countries.

Samir El QaidiCollege of Veterinary Medicine, Kansas State University, Manhattan, KS, 66506, USA.
Nichollas E ScottDepartment of Microbiology and Immunology, University of Melbourne within the Peter Doherty Institute for Infection and Immunity, Melbourne, 3000, Australia.
Michael P HaysCollege of Veterinary Medicine, Kansas State University, Manhattan, KS, 66506, USA.
Brian V GeisbrechtDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS, 66506, USA.
Shelby WatkinsCollege of Veterinary Medicine, Kansas State University, Manhattan, KS, 66506, USA.
Philip R HardwidgeCollege of Veterinary Medicine, Kansas State University, Manhattan, KS, 66506, USA. hardwidg@vet.k-state.edu.
Kansas State University · USPeter Doherty Institute · AU

Funding

Functions of Translocated Bacterial GlycosyltransferasesR21AI127973 · NIAID · KANSAS STATE UNIVERSITY · PI HARDWIDGE, PHILIP ROSS · 2017 to 2018
$413k
NIAID NIH HHS R21 AI127973
6 · The paper itself

Abstract

Many Gram-negative bacterial pathogens interact with mammalian cells by using type III secretion systems (T3SS) to inject virulence proteins into host cells. A subset of these injected protein 'effectors' are enzymes that inhibit the function of host proteins by catalyzing the addition of unusual post-translational modifications. The E. coli and Citrobacter rodentium NleB effectors, as well as the Salmonella enterica SseK effectors are glycosyltransferases that modify host protein substrates with N-acetyl glucosamine (GlcNAc) on arginine residues. This post-translational modification disrupts the normal functioning of host immune response proteins. T3SS effectors are thought to be inactive within the bacterium and fold into their active conformations after they are injected, due to the activity of chaperones that keep the effectors in a structural state permissive for secretion. While performing mass spectrometry experiments to identify glycosylation substrates of NleB orthologs, we unexpectedly observed that the bacterial glutathione synthetase (GshB) is glycosylated by NleB on arginine residue R256. NleB-mediated glycosylation of GshB resulted in enhanced GshB activity, leading to an increase in glutathione production, and promoted C. rodentium survival in oxidative stress conditions. These data represent, to our knowledge, the first intra-bacterial activity for a T3SS effector and show that arginine-GlcNAcylation, once thought to be restricted to host cell compartments, also plays an important role in regulating bacterial physiology.

Indexed as

Bacterial ProteinsCitrobacter rodentiumGlycosylationSalmonella entericaType III Secretion SystemsBacterial ProteinsType III Secretion Systems

Identifiers

PMID31974499
PMCPMC6978387
OpenAlexW3002426628

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.