Evidence map›Paper›PMID 31611039›Full record

ArticleStructure (London, England : 1993)2019

Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles.

Matthew J Byrne, John F C Steele, Emma L Hesketh, Miriam Walden, Rebecca F Thompson, George P Lomonossoff, Neil A Ranson

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. The Journal of general virology · 2026
    Article
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  8. ICTV Virus Taxonomy Profile:The Journal of general virology · 2021
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Matthew J ByrneAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
John F C SteeleDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK.
Emma L HeskethAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
Miriam WaldenDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK.
Rebecca F ThompsonAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
George P LomonossoffDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK. Electronic address: george.lomonossoff@jic.ac.uk.
Neil A RansonAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK. Electronic address: n.a.ranson@leeds.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/J004596/1Biotechnology and Biological Sciences Research Council BB/L014130/1Biotechnology and Biological Sciences Research Council BB/L020955/1Biotechnology and Biological Sciences Research Council BB/R00160X/1Biotechnology and Biological Sciences Research Council BBS/E/000PR9794Wellcome Trust 108466Wellcome Trust 108466/Z/15/Z
6 · The paper itself

Abstract

The Luteoviridae are pathogenic plant viruses responsible for significant crop losses worldwide. They infect a wide range of food crops, including cereals, legumes, cucurbits, sugar beet, sugarcane, and potato and, as such, are a major threat to global food security. Viral replication is strictly limited to the plant vasculature, and this phloem limitation, coupled with the need for aphid transmission of virus particles, has made it difficult to generate virus in the quantities needed for high-resolution structural studies. Here, we exploit recent advances in heterologous expression in plants to produce sufficient quantities of virus-like particles for structural studies. We have determined their structures to high resolution by cryoelectron microscopy, providing the molecular-level insight required to rationally interrogate luteovirid capsid formation and aphid transmission, thereby providing a platform for the development of preventive agrochemicals for this important family of plant viruses.

Indexed as

Amino Acid SequenceAnimalsAphidsCapsidCapsid ProteinsCryoelectron MicroscopyGene Expression Regulation, ViralInsect VectorsLuteoviridaePhloemPlant DiseasesPlant VirusesProtein ConformationSequence Homology, Amino AcidVirionCapsid Proteinscryo-EMhomology modelingluteovirusplant virusstructurevirus

Identifiers

PMID31611039
PMCPMC6899511

What OpenQuestion holds

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LicenceCC BY
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.