Evidence map›Paper›PMID 27647866›Full record

ArticleInfection and immunity2016

Thermal Unfolding of the Pertussis Toxin S1 Subunit Facilitates Toxin Translocation to the Cytosol by the Mechanism of Endoplasmic Reticulum-Associated Degradation.

Tuhina Banerjee, Lucia Cilenti, Michael Taylor, Adrienne Showman, Suren A Tatulian, Ken Teter

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2016. 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
0.9field-weighted citation impact, top 25% 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, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. An endogenous human peptide derived from αNaunyn-Schmiedeberg's archives of pharmacology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Domperidone InhibitsToxins · 2023
    Article
  9. Article
  10. Targeting the Inside of Cells with Biologicals: Toxin Routes in a Therapeutic Context.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023
    Review
  11. Article
  12. Crystal structures of pertussis toxin with NADThe Journal of biological chemistry · 2022
    Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. International journal of molecular sciences · 2021
    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

6 authors at 1 institution in 1 country.

Tuhina BanerjeeBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida, USA.
Lucia CilentiBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida, USA.
Michael TaylorBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida, USA.
Adrienne ShowmanBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida, USA.
Suren A TatulianDepartment of Physics, University of Central Florida, Orlando, Florida, USA.
Ken TeterBurnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida, USA kteter@mail.ucf.edu.
University of Central Florida · US

Funding

A Novel Mechanism for Toxin Export from the Endoplasmic Reticulum to the CytosolR01AI099493 · NIAID · UNIVERSITY OF CENTRAL FLORIDA · PI TETER, KENNETH R · 2012 to 2016
$1.9M
NIAID NIH HHS R01 AI099493
6 · The paper itself

Abstract

Pertussis toxin (PT) moves from the host cell surface to the endoplasmic reticulum (ER) by retrograde vesicular transport. The catalytic PTS1 subunit dissociates from the rest of the toxin in the ER and then shifts to a disordered conformation which may trigger its export to the cytosol through the quality control mechanism of ER-associated degradation (ERAD). Functional roles for toxin instability and ERAD in PTS1 translocation have not been established. We addressed these issues with the use of a surface plasmon resonance system to quantify the cytosolic pool of PTS1 from intoxicated cells. Only 3% of surface-associated PTS1 reached the host cytosol after 3 h of toxin exposure. This represented, on average, 38,000 molecules of cytosolic PTS1 per cell. Cells treated with a proteasome inhibitor contained larger quantities of cytosolic PTS1. Stabilization of the dissociated PTS1 subunit with chemical chaperones inhibited toxin export to the cytosol and blocked PT intoxication. ERAD-defective cell lines likewise exhibited reduced quantities of cytosolic PTS1 and PT resistance. These observations identify the unfolding of dissociated PTS1 as a trigger for its ERAD-mediated translocation to the cytosol.

Indexed as

AnimalsCHO CellsCricetulusCytosolEndoplasmic Reticulum-Associated DegradationGene Expression RegulationHot TemperatureMolecular ChaperonesPertussis ToxinProtein TransportProtein UnfoldingMolecular ChaperonesPertussis Toxinpertussis toxin, S1 subunit

Identifiers

PMID27647866
PMCPMC5116717
OpenAlexW2522383607

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.