Evidence map›Paper›PMID 11070038›Full record

ArticleJournal of virology2000

Glycoprotein E of varicella-zoster virus enhances cell-cell contact in polarized epithelial cells.

C Mo, E E Schneeberger, A M Arvin

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 51 citations in OpenAlex.

  1. Trial
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  9. Frontiers in microbiology · 2022
    Review
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  14. Review
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  16. Article
  17. Functions of the unique N-terminal region of glycoprotein E in the pathogenesis of varicella-zoster virus infection.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  18. Article
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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

3 authors at 2 institutions in 1 country.

C MoDepartment of Pediatrics, Stanford University School of Medicine, Stanford, California 94305, USA. cmo@cmgm.stanford.edu
E E Schneeberger
A M Arvin
Stanford University · USMassachusetts General Hospital · US

Funding

Varicella-Zoster Virus: T Cell/Skin Tropisms &ImmunityR01AI020459 · NIAID · STANFORD UNIVERSITY · PI OLIVER, STEFAN LYNE · 1985 to 2023
$6.4M
Varicella-Zoster Virus: T Cell/Skin Tropisms & ImmunityR37AI020459 · NIAID · STANFORD UNIVERSITY · PI ARVIN, ANN · 2016 to 2020
$2.0M
NIAID NIH HHS AI20459NIAID NIH HHS R01 AI020459NIAID NIH HHS R37 AI020459
6 · The paper itself

Abstract

Varicella-zoster virus (VZV) infection involves the cell-cell spread of virions, but how viral proteins interact with the host cell membranes that comprise intercellular junctions is not known. Madin-Darby canine kidney (MDCK) cells were constructed to express the glycoproteins gE, gI, or gE/gI constitutively and were used to examine the effects of these VZV glycoproteins in polarized epithelial cells. At low cell density, VZV gE induced partial tight junction (TJ) formation under low-calcium conditions, whether expressed alone or with gI. Although most VZV gE was intracellular, gE was also shown to colocalize with the TJ protein ZO-1 with or without concomitant expression of gI. Freeze fracture electron microscopy revealed normal TJ strand morphology in gE-expressing MDCK cells. Functionally, the expression of gE was associated with a marked acceleration in the establishment of maximum transepithelial electrical resistance (TER) in MDCK-gE cells; MDCK-gI and MDCK-gE/gI cells exhibited a similar pattern of early TER compared to MDCK cells, although peak resistances were lower than those of gE alone. VZV gE expression altered F-actin organization and lipid distribution, but coexpression of gI modulated these effects. Two regions of the gE ectodomain, amino acids (aa) 278 to 355 and aa 467 to 498, although lacking Ca(2+) binding motifs, exhibit similarities with corresponding regions of the cell adhesion molecules, E-cadherin and desmocollin. These observations suggest that VZV gE and gE/gI may contribute to viral pathogenesis by facilitating epithelial cell-cell contacts.

Indexed as

Cell CommunicationActinsAmino Acid SequenceAnimalsCadherinsCell LineCell PolarityCytoskeletal ProteinsDesmocollinsDesmoplakinsDogsElectric ImpedanceEpithelial CellsHerpesvirus 3, HumanLipidsMolecular Sequence DataActinsCadherinsCytoskeletal ProteinsDesmocollinsDesmoplakinsglycoprotein E, varicella-zoster virusLipidsViral Envelope Proteins

Identifiers

PMID11070038
PMCPMC113243
OpenAlexW2118594039

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.