Evidence map›Paper›PMID 25787255›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization.

Elaine Chiu, Marcel Hijnen, Richard D Bunker, Marion Boudes, Chitra Rajendran, Kaheina Aizel, Vincent Oliéric, Clemens Schulze-Briese, Wataru Mitsuhashi, Vivienne Young and 4 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
7.8field-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

40 citing papers in PubMed, 106 citations in OpenAlex.

  1. Chemical reviews · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. High-throughput structure determination of an intrinsically disordered protein using cell-free protein crystallization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. The disordered C-terminal tail of fungal LPMOs from phytopathogens mediates protein dimerization and impacts plant penetration.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. TheApplied and environmental microbiology · 2023
    Article
  11. Article
  12. Characterization of a unique polysaccharide monooxygenase from the plant pathogenProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Review
  14. Article
  15. Orchestrating copper binding: structure and variations on the cupredoxin fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  16. Article
  17. Chitin-Active Lytic Polysaccharide Monooxygenases Are Rare inApplied and environmental microbiology · 2022
    Article
  18. Article
  19. 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

14 authors at 7 institutions in 5 countries.

Elaine ChiuSchool of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand;
Marcel HijnenDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia;
Richard D BunkerSchool of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand;
Marion BoudesDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia;
Chitra RajendranSwiss Light Source at Paul Scherrer Institut, 5232 Villigen, Switzerland;
Kaheina AizelDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia;
Vincent OliéricSwiss Light Source at Paul Scherrer Institut, 5232 Villigen, Switzerland;
Clemens Schulze-BrieseSwiss Light Source at Paul Scherrer Institut, 5232 Villigen, Switzerland;
Wataru MitsuhashiNational Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8634, Japan;
Vivienne YoungDepartment of Microbiology and Immunology, School of Medical Sciences, University of Otago, Dunedin, 9054, New Zealand; and.
Vernon K WardDepartment of Microbiology and Immunology, School of Medical Sciences, University of Otago, Dunedin, 9054, New Zealand; and.
Max BergoinUniversité Montpellier 2, Montpellier 34095, France.
Peter MetcalfSchool of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand; fasseli.coulibaly@monash.edu peter.metcalf@auckland.ac.nz.
Fasséli CoulibalyDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia; fasseli.coulibaly@monash.edu peter.metcalf@auckland.ac.nz.
Monash University · AUUniversity of Auckland · NZPaul Scherrer Institute · CHUniversity of Otago · NZInstitute of Agrobiological Sciences · JPSwiss Light SourceUniversité de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The great benefits that chemical pesticides have brought to agriculture are partly offset by widespread environmental damage to nontarget species and threats to human health. Microbial bioinsecticides are considered safe and highly specific alternatives but generally lack potency. Spindles produced by insect poxviruses are crystals of the fusolin protein that considerably boost not only the virulence of these viruses but also, in cofeeding experiments, the insecticidal activity of unrelated pathogens. However, the mechanisms by which spindles assemble into ultra-stable crystals and enhance virulence are unknown. Here we describe the structure of viral spindles determined by X-ray microcrystallography from in vivo crystals purified from infected insects. We found that a C-terminal molecular arm of fusolin mediates the assembly of a globular domain, which has the hallmarks of lytic polysaccharide monooxygenases of chitinovorous bacteria. Explaining their unique stability, a 3D network of disulfide bonds between fusolin dimers covalently crosslinks the entire crystalline matrix of spindles. However, upon ingestion by a new host, removal of the molecular arm abolishes this stabilizing network leading to the dissolution of spindles. The released monooxygenase domain is then free to disrupt the chitin-rich peritrophic matrix that protects insects against oral infections. The mode of action revealed here may guide the design of potent spindles as synergetic additives to bioinsecticides.

Indexed as

Amino Acid SequenceAnimalsCatalytic DomainChitinCrystallizationCrystallography, X-RayDisulfidesInsectaInsecticidesMacromolecular SubstancesMixed Function OxygenasesModels, MolecularMolecular Sequence DataOxygenOxygenasesPolysaccharidesChitinDisulfidesfusolin protein, entomopoxvirusInsecticidesMacromolecular SubstancesMixed Function OxygenasesOxygenOxygenasesPolysaccharidesViral ProteinsVirulence Factorsin vivo crystallizationLPMOmicrocrystallographypesticidepoxvirus

Identifiers

PMID25787255
PMCPMC4386404
OpenAlexW2171092594

What OpenQuestion holds

Textmetadata
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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.