Evidence map›Paper›PMID 24567401›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Self-assembly of the general membrane-remodeling protein PVAP into sevenfold virus-associated pyramids.

Bertram Daum, Tessa E F Quax, Martin Sachse, Deryck J Mills, Julia Reimann, Özkan Yildiz, Sabine Häder, Cosmin Saveanu, Patrick Forterre, Sonja-Verena Albers and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Viruses of theFrontiers in microbiology · 2023
    Review
  6. Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022
    Article
  7. Review
  8. Article
  9. A filamentous archaeal virus is enveloped inside the cell and released through pyramidal portals.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Architecture and modular assembly ofProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. The enigmatic archaeal virosphere.Nature reviews. Microbiology · 2017
    Review
  18. Article
  19. Structure andeLife · 2017
    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

12 authors at 4 institutions in 2 countries.

Bertram DaumDepartment of Structural Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.
Tessa E F Quax
Martin Sachse
Deryck J Mills
Julia Reimann
Özkan Yildiz
Sabine Häder
Cosmin Saveanu
Patrick Forterre
Sonja-Verena Albers
Werner Kühlbrandt
David Prangishvili
Max Planck Institute of Biophysics · DEBiology of Extremophiles Laboratory · FRMax Planck Institute for Terrestrial Microbiology · DEInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viruses have developed a wide range of strategies to escape from the host cells in which they replicate. For egress some archaeal viruses use a pyramidal structure with sevenfold rotational symmetry. Virus-associated pyramids (VAPs) assemble in the host cell membrane from the virus-encoded protein PVAP and open at the end of the infection cycle. We characterize this unusual supramolecular assembly using a combination of genetic, biochemical, and electron microscopic techniques. By whole-cell electron cryotomography, we monitored morphological changes in virus-infected host cells. Subtomogram averaging reveals the VAP structure. By heterologous expression of PVAP in cells from all three domains of life, we demonstrate that the protein integrates indiscriminately into virtually any biological membrane, where it forms sevenfold pyramids. We identify the protein domains essential for VAP formation in PVAP truncation mutants by their ability to remodel the cell membrane. Self-assembly of PVAP into pyramids requires at least two different, in-plane and out-of-plane, protein interactions. Our findings allow us to propose a model describing how PVAP arranges to form sevenfold pyramids and suggest how this small, robust protein may be used as a general membrane-remodeling system.

Indexed as

Models, MolecularProtein ConformationCell MembraneCryoelectron MicroscopyEscherichia coliMultiprotein ComplexesPlasmidsRudiviridaeSaccharomyces cerevisiaeSulfolobusViral ProteinsVirus ReleaseMultiprotein ComplexesViral Proteinsarchaeaarcheovirusviral egress

Identifiers

PMID24567401
PMCPMC3956195
OpenAlexW2064822149

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.