Evidence map›Paper›PMID 31328164›Full record

ArticleScience advances2019

Structural basis for the multitasking nature of the potato virus Y coat protein.

Andreja Kežar, Luka Kavčič, Martin Polák, Jiří Nováček, Ion Gutiérrez-Aguirre, Magda Tušek Žnidarič, Anna Coll, Katja Stare, Kristina Gruden, Maja Ravnikar and 5 more

Abstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
–field-weighted citation impact
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

42 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Rational design of 2iScience · 2024
    Article
  16. 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

15 authors.

Andreja KežarDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.ORCID 0000-0003-2407-9297
Luka KavčičDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.ORCID 0000-0002-2665-3582
Martin PolákCentral European Institute of Technology, Masaryk University, Kamenice 753/5, Brno 625 00, Czech Republic.ORCID 0000-0001-6724-6222
Jiří NováčekCentral European Institute of Technology, Masaryk University, Kamenice 753/5, Brno 625 00, Czech Republic.ORCID 0000-0003-4013-3898
Ion Gutiérrez-AguirreDepartment of Biotechnology and Systems Biology, National Institute of Biology, Večna pot 111, 1000 Ljubljana, Slovenia.ORCID 0000-0002-8348-8616
Magda Tušek ŽnidaričDepartment of Biotechnology and Systems Biology, National Institute of Biology, Večna pot 111, 1000 Ljubljana, Slovenia.ORCID 0000-0002-4349-3752
Anna CollDepartment of Biotechnology and Systems Biology, National Institute of Biology, Večna pot 111, 1000 Ljubljana, Slovenia.ORCID 0000-0003-0672-1530
Katja StareDepartment of Biotechnology and Systems Biology, National Institute of Biology, Večna pot 111, 1000 Ljubljana, Slovenia.ORCID 0000-0002-3999-9400
Kristina GrudenDepartment of Biotechnology and Systems Biology, National Institute of Biology, Večna pot 111, 1000 Ljubljana, Slovenia.ORCID 0000-0001-5906-8569
Maja RavnikarDepartment of Biotechnology and Systems Biology, National Institute of Biology, Večna pot 111, 1000 Ljubljana, Slovenia.ORCID 0000-0002-6630-1362
David PahovnikDepartment of Polymer Chemistry and Technology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.ORCID 0000-0001-8024-8871
Ema ŽagarDepartment of Polymer Chemistry and Technology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.ORCID 0000-0002-2694-4312
Franci MerzelTheory Department, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.ORCID 0000-0002-2748-4901
Gregor AnderluhDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.ORCID 0000-0002-9916-8465
Marjetka PodobnikDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.ORCID 0000-0001-6786-9737

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Potato virus Y (PVY) is among the most economically important plant pathogens. Using cryoelectron microscopy, we determined the near-atomic structure of PVY's flexuous virions, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA. RNA-coat protein interactions are crucial for the helical configuration and stability of the virion, as revealed by the unique near-atomic structure of RNA-free virus-like particles. The structures offer the first evidence for plasticity of the coat protein's amino- and carboxyl-terminal regions. Together with mutational analysis and in planta experiments, we show their crucial role in PVY infectivity and explain the ability of the coat protein to perform multiple biological tasks. Moreover, the high modularity of PVY virus-like particles suggests their potential as a new molecular scaffold for nanobiotechnological applications.

Indexed as

Models, MolecularProtein ConformationAmino Acid SequenceBinding SitesCapsidCapsid ProteinsPlant DiseasesPotyvirusProtein BindingRNA, ViralStructure-Activity RelationshipVirionCapsid Proteinscoat protein, Potato virus YRNA, Viral

Identifiers

PMID31328164
PMCPMC6636993

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.