Evidence map›Paper›PMID 19864391›Full record

ArticleJournal of virology2010

Insulin-degrading enzyme binds to the nonglycosylated precursor of varicella-zoster virus gE protein found in the endoplasmic reticulum.

J E Carpenter, W Jackson, G A de Souza, L Haarr, C Grose

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Frontiers in microbiology · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Pathogenesis of varicelloviruses in primates.The Journal of pathology · 2015
    Review
  16. Article
  17. Article
  18. Proteolytic degradation of amyloid β-protein.Cold Spring Harbor perspectives in medicine · 2012
    Review
  19. 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

5 authors at 2 institutions in 2 countries.

J E CarpenterChildren's Hospital, University of Iowa, Iowa City, Iowa 52242, USA.
W Jackson
G A de Souza
L Haarr
C Grose
University of Iowa Stead Family Children’s Hospital · USUniversity of Bergen · NO

Funding

Varicella-zoster Virus: Tegument Proteins in PathogenesisR01AI053846 · NIAID · STANFORD UNIVERSITY · PI ARVIN, ANN · 2003 to 2012
$4.1M
NIAID NIH HHS AI53846NIAID NIH HHS R01 AI053846
6 · The paper itself

Abstract

Insulin degradation enzyme (IDE) is a 110-kDa zinc metalloprotease found in the cytosol of all cells. IDE degrades insulin and a variety of small proteins including amyloid-beta. Recently, IDE has been proposed as the receptor for varicella-zoster virus (VZV) attachment. During our reassessment, some of the original studies were repeated and expanded in scope. We first confirmed that IDE antibody reduced VZV spread. For additional controls, we repeated the same experiments with herpes simplex virus (HSV)-infected cells as well as uninfected cells. There was a visible reduction in HSV spread but less than seen in the VZV system. Of greater importance, IDE antibody also inhibited the growth of uninfected cells. Second, we repeated the coprecipitation assays. We confirmed that antibodies to VZV gE (open reading frame 68) coprecipitated IDE and that anti-IDE antibody coprecipitated gE. However, the detected gE protein was not the mature 98-kDa form; rather, it was a precursor 73-kDa gE form found in the endoplasmic reticulum. Additional control experiments included VZV-infected cell cultures treated with tunicamycin to block gE glycosylation in the endoplasmic reticulum; again, the anti-IDE antibody coprecipitated a 73-kDa gE product. Finally, Orbitrap mass spectrometry analysis of a chromatographically purified gE sample revealed four cellular proteins associated with the unfolded protein response: BiP (HSPA5), HSPA8, HSPD1, and PPIA (peptidyl-propyl cis-trans isomerase). We conclude that IDE protease binds to the 73-kDa gE precursor and that this event occurs in the cytosol but not as a receptor/ligand interaction.

Indexed as

AnimalsCell Line, TumorChild, PreschoolEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPHerpesvirus 3, HumanHumansInsulysinProtein PrecursorsUnfolded Protein ResponseViral Envelope ProteinsEndoplasmic Reticulum Chaperone BiPglycoprotein E, varicella-zoster virusHSPA5 protein, humanInsulysinProtein PrecursorsViral Envelope Proteins

Identifiers

PMID19864391
PMCPMC2798375
OpenAlexW2100419117

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.