Evidence map›Paper›PMID 22919642›Full record

ReviewFrontiers in cellular and infection microbiology2012

Insights on the trafficking and retro-translocation of glycosphingolipid-binding bacterial toxins.

Jin A Cho, Daniel J-F Chinnapen, Emil Aamar, Yvonne M te Welscher, Wayne I Lencer, Ramiro Massol

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cellular and infection microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-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

33 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. The diverse landscape of AB5-type toxins.Engineering microbiology · 2023
    Review
  3. Review
  4. Review
  5. EnterohemorrhagicInternational journal of molecular sciences · 2022
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Intracellular trafficking of bacterial toxins.Current opinion in cell biology · 2016
    Review
  18. Article
  19. Article
  20. Membrane Tethering Complexes in the Endosomal System.Frontiers in cell and developmental biology · 2016
    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 3 institutions in 1 country.

Jin A ChoDivision of Gastroenterology and Nutrition, Department of Medicine, Children's Hospital Boston, Boston MA, USA; Department of Pediatrics, Harvard Medical School, Boston, MA, USA.
Daniel J-F Chinnapen
Emil Aamar
Yvonne M te Welscher
Wayne I Lencer
Ramiro Massol
Boston University · USBoston Children's Hospital · USHarvard University · US

Funding

FcRn-dependent sorting of IgG and IgG-opsinized antigens by epithelial cellsR01DK084424 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI LENCER, WAYNE I · 2009 to 2013
$1.9M
NIDDK NIH HHS R01 DK084424
6 · The paper itself

Abstract

Some bacterial toxins and viruses have evolved the capacity to bind mammalian glycosphingolipids to gain access to the cell interior, where they can co-opt the endogenous mechanisms of cellular trafficking and protein translocation machinery to cause toxicity. Cholera toxin (CT) is one of the best-studied examples, and is the virulence factor responsible for massive secretory diarrhea seen in cholera. CT enters host cells by binding to monosialotetrahexosylganglioside (GM1 gangliosides) at the plasma membrane where it is transported retrograde through the trans-Golgi network (TGN) into the endoplasmic reticulum (ER). In the ER, a portion of CT, the CT-A1 polypeptide, is unfolded and then "retro-translocated" to the cytosol by hijacking components of the ER associated degradation pathway (ERAD) for misfolded proteins. CT-A1 rapidly refolds in the cytosol, thus avoiding degradation by the proteasome and inducing toxicity. Here, we highlight recent advances in our understanding of how the bacterial AB(5) toxins induce disease. We highlight the molecular mechanisms by which these toxins use glycosphingolipid to traffic within cells, with special attention to how the cell senses and sorts the lipid receptors. We also discuss several new studies that address the mechanisms of toxin unfolding in the ER and the mechanisms of CT A1-chain retro-translocation to the cytosol.

Indexed as

AnimalsBacterial ToxinsCell MembraneCytosolEndoplasmic ReticulumEukaryotic CellsGlycosphingolipidsGolgi ApparatusHumansMammalsProtein BindingProtein TransportBacterial ToxinsGlycosphingolipidscholera toxinERADmembrane traffickingretro-translocation

Identifiers

PMID22919642
PMCPMC3417474
OpenAlexW2096038670

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.