Evidence map›Paper›PMID 15613328›Full record

ArticleJournal of virology2005

Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope.

Lucie Maresova, Tracy Jo Pasieka, Elizabeth Homan, Erick Gerday, Charles Grose

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Adjuvanted Recombinant Glycoprotein E Herpes Zoster Vaccine.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2020
    Article
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  19. 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
  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

5 authors at 1 institution in 1 country.

Lucie MaresovaUniversity of Iowa Hospital/2501 JCP, 200 Hawkins Dr., Iowa City, IA 52242, USA.
Tracy Jo Pasieka
Elizabeth Homan
Erick Gerday
Charles Grose
University of Iowa · US

Funding

UI INITIATIVE FOR MINORITY STUDENT DEVELOPMENT PROGRAMR25GM058939 · NIGMS · UNIVERSITY OF IOWA · PI ADAMS-PHILLIPS, LORI C, FORBES, TORI · 1999 to 2021
$6.9M
RESEARCH TRAINING IN INFECTIOUS DISEASEST32AI007343 · NIAID · UNIVERSITY OF IOWA · PI STAPLETON, JACK T. · 1988 to 2024
$5.0M
ANTIGENIC DETERMINANTS OF VARICELLA VIRUSR01AI022795 · NIAID · UNIVERSITY OF IOWA · PI GROSE, CHARLES F. · 1985 to 2006
$2.4M
NIAID NIH HHS R01 AI022795NIAID NIH HHS R01 AI22795NIAID NIH HHS R32 AI 07343NIAID NIH HHS T32 AI007343NIGMS NIH HHS R25 GM058939NIGMS NIH HHS R25 GM 58939
6 · The paper itself

Abstract

The cytoplasmic tails of all three major varicella-zoster virus (VZV) glycoproteins, gE, gH, and gB, harbor functional tyrosine-based endocytosis motifs that mediate internalization. The aim of the present study was to examine whether endocytosis from the plasma membrane is a cellular route by which VZV glycoproteins are delivered to the final envelopment compartment. In this study, we demonstrated that internalization of the glycoproteins occurred in the first 24 h postinfection but was reduced later in infection. Using surface biotinylation of VZV-infected cells followed by a glutathione cleavage assay, we showed that endocytosis was independent of antibody binding to gE, gH, and gB. Subsequently, with this assay, we demonstrated that biotinylated gE, gH, and gB retrieved from the cell surface were incorporated into nascent virus particles isolated after density gradient sedimentation. To confirm and extend this finding, we repeated the above sedimentation step and specifically detected envelopes decorated with Streptavidin-conjugated gold beads on a majority of complete virions through examination by transmission electron microscopy. In addition, a gE-gI complex and a gE-gH complex were found on the virions. Therefore, the above studies established that VZV subsumed a postendocytosis trafficking pathway as one mechanism by which to deliver viral glycoproteins to the site of virion assembly in the cytoplasm. Furthermore, since a recombinant VZV genome lacking only endocytosis-competent gE cannot replicate, these results supported the conclusion that the endocytosis-envelopment pathway is an essential component of the VZV life cycle.

Indexed as

EndocytosisBiotinylationCell Line, TumorCell MembraneHerpesvirus 3, HumanHumansMembrane GlycoproteinsMicroscopy, ElectronViral Envelope ProteinsViral ProteinsVirionglycoprotein B, varicella-zoster virusglycoprotein E, varicella-zoster virusgp 118 protein, Herpesvirus 3, HumanMembrane GlycoproteinsViral Envelope ProteinsViral Proteins

Identifiers

PMID15613328
PMCPMC538533
OpenAlexW2060788847

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.