Evidence map›Paper›PMID 19158241›Full record

ArticleJournal of virology2009

Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase.

Todd W Wisner, Catherine C Wright, Akihisa Kato, Yasushi Kawaguchi, Fan Mou, Joel D Baines, Richard J Roller, David C Johnson

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
6.9field-weighted citation impact, top 3% 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

69 citing papers in PubMed, 107 citations in OpenAlex.

  1. Review
  2. Article
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  6. Article
  7. Article
  8. Antiviral Effect of Polyphenolic Substances inEvidence-based complementary and alternative medicine : eCAM · 2022
    Article
  9. Review
  10. Article
  11. Review
  12. Nuclear Egress.Current issues in molecular biology · 2021
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

9 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 2 countries.

Todd W WisnerDepartment of Molecular Microbiology & Immunology, Oregon Health & Sciences University, Portland, Oregon 97239, USA.
Catherine C Wright
Akihisa Kato
Yasushi Kawaguchi
Fan Mou
Joel D Baines
Richard J Roller
David C Johnson
Oregon Health & Science University · USCornell University · USTokyo University of Science · JPUniversity of Iowa · US

Funding

Herpes simplex virus egress from neurons into axons mediated by HSV membrane proteins gE/gI and US9 and axonal transport by kinesin motors.R01EY018755 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI JOHNSON, DAVID C. · 2008 to 2023
$5.8M
UL34 AND HERPES SIMPLEX VIRUS INFECTIONR01AI041478 · NIAID · UNIVERSITY OF IOWA · PI ROLLER, RICHARD J · 1999 to 2010
$2.0M
NEI NIH HHS EY018755-11NEI NIH HHS R01 EY018755NIAID NIH HHS AI 41478NIAID NIH HHS AI 52431NIAID NIH HHS R01 AI041478
6 · The paper itself

Abstract

Herpesvirus capsids collect along the inner surface of the nuclear envelope and bud into the perinuclear space. Enveloped virions then fuse with the outer nuclear membrane (NM). We previously showed that herpes simplex virus (HSV) glycoproteins gB and gH act in a redundant fashion to promote fusion between the virion envelope and the outer NM. HSV mutants lacking both gB and gH accumulate enveloped virions in herniations, vesicles that bulge into the nucleoplasm. Earlier studies had shown that HSV mutants lacking the viral serine/threonine kinase US3 also accumulate herniations. Here, we demonstrate that HSV gB is phosphorylated in a US3-dependent manner in HSV-infected cells, especially in a crude nuclear fraction. Moreover, US3 directly phosphorylated the gB cytoplasmic (CT) domain in in vitro assays. Deletion of gB in the context of a US3-null virus did not add substantially to defects in nuclear egress. The majority of the US3-dependent phosphorylation of gB involved the CT domain and amino acid T887, a residue present in a motif similar to that recognized by US3 in other proteins. HSV recombinants lacking gH and expressing either gB substitution mutation T887A or a gB truncated at residue 886 displayed substantial defects in nuclear egress. We concluded that phosphorylation of the gB CT domain is important for gB-mediated fusion with the outer NM. This suggested a model in which the US3 kinase is incorporated into the tegument layer (between the capsid and envelope) in HSV virions present in the perinuclear space. By this packaging, US3 might be brought close to the gB CT tail, leading to phosphorylation and triggering fusion between the virion envelope and the outer NM.

Indexed as

Virus InternalizationAmino Acid SubstitutionAnimalsCell LineHerpesvirus 1, HumanHumansModels, BiologicalMutagenesis, Site-DirectedNuclear EnvelopePhosphorylationProtein Serine-Threonine KinasesSequence DeletionViral Envelope ProteinsViral ProteinsVirionglycoprotein B, SimplexvirusProtein Serine-Threonine KinasesUS3 protein, Human herpesvirus 1Viral Envelope ProteinsViral Proteins

Identifiers

PMID19158241
PMCPMC2655551
OpenAlexW2143813693

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.