Evidence map›Paper›PMID 25605719›Full record

ArticleThe Journal of biological chemistry2015

A single herpesvirus protein can mediate vesicle formation in the nuclear envelope.

Michael Lorenz, Benjamin Vollmer, Joseph D Unsay, Barbara G Klupp, Ana J García-Sáez, Thomas C Mettenleiter, Wolfram Antonin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

53 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanisms for assembly of the nucleoplasmic reticulum.Cellular and molecular life sciences : CMLS · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Nuclear Egress.Current issues in molecular biology · 2021
    Review
  15. Review
  16. Quantitative Electron Microscopy to Study HCMV Morphogenesis.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  17. Article
  18. Article
  19. Review
  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

7 authors at 3 institutions in 1 country.

Michael LorenzFrom the Friedrich Miescher Laboratory of the Max Planck Society, 72076 Tübingen, Germany.
Benjamin VollmerFrom the Friedrich Miescher Laboratory of the Max Planck Society, 72076 Tübingen, Germany.
Joseph D Unsaythe Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany, and.
Barbara G Kluppthe Friedrich Loeffler Institute, Federal Research Institute for Animal Health, 17493 Greifswald, Germany.
Ana J García-Sáezthe Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany, and.
Thomas C Mettenleiterthe Friedrich Loeffler Institute, Federal Research Institute for Animal Health, 17493 Greifswald, Germany.
Wolfram AntoninFrom the Friedrich Miescher Laboratory of the Max Planck Society, 72076 Tübingen, Germany, wolfram.antonin@tuebingen.mpg.de.
Max Planck Society · DEFriedrich-Loeffler-Institut · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herpesviruses assemble capsids in the nucleus and egress by unconventional vesicle-mediated trafficking through the nuclear envelope. Capsids bud at the inner nuclear membrane into the nuclear envelope lumen. The resulting intralumenal vesicles fuse with the outer nuclear membrane, delivering the capsids to the cytoplasm. Two viral proteins are required for vesicle formation, the tail-anchored pUL34 and its soluble interactor, pUL31. Whether cellular proteins are involved is unclear. Using giant unilamellar vesicles, we show that pUL31 and pUL34 are sufficient for membrane budding and scission. pUL34 function can be bypassed by membrane tethering of pUL31, demonstrating that pUL34 is required for pUL31 membrane recruitment but not for membrane remodeling. pUL31 can inwardly deform membranes by oligomerizing on their inner surface to form buds that constrict to vesicles. Therefore, a single viral protein can mediate all events necessary for membrane budding and abscission.

Indexed as

Host-Pathogen InteractionsAnimalsBiological TransportHerpesvirus 1, SuidLipid BilayersLiposomesNuclear EnvelopePseudorabiesSwineViral ProteinsVirus ReleaseLipid BilayersLiposomesViral ProteinsHerpesvirusMembrane ReconstitutionMembrane TraffickingNuclear EnvelopeNuclear Translocation

Identifiers

PMID25605719
PMCPMC4358120
OpenAlexW2076330310

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.