Evidence map›Paper›PMID 29706532›Full record

ArticleStructure (London, England : 1993)2018

The Structure of an Infectious Human Polyomavirus and Its Interactions with Cellular Receptors.

Daniel L Hurdiss, Martin Frank, Joseph S Snowden, Andrew Macdonald, Neil A Ranson

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Ribosomal protein S25 promotes cell cycle entry for a productive BK polyomavirus infection.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  4. Article
  5. Review
  6. The Conserved YPXViruses · 2024
    Article
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  8. Review
  9. Article
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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

5 authors at 2 institutions in 2 countries.

Daniel L HurdissAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
Martin FrankBiognos AB, P.O. Box 8963, Gothenburg 40274, Sweden.
Joseph S SnowdenAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
Andrew MacdonaldAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK. Electronic address: a.macdonald@leeds.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.
University of Leeds · GBBiognos (Sweden) · SE

Funding

Wellcome Trust 108466
6 · The paper itself

Abstract

BK polyomavirus (BKV) causes polyomavirus-associated nephropathy and hemorrhagic cystitis in immunosuppressed patients. These are diseases for which we currently have limited treatment options, but potential therapies could include pre-transplant vaccination with a multivalent BKV vaccine or therapeutics which inhibit capsid assembly or block attachment and entry into target cells. A useful tool in such efforts would be a high-resolution structure of the infectious BKV virion and how this interacts with its full repertoire of cellular receptors. We present the 3.4-Å cryoelectron microscopy structure of native, infectious BKV in complex with the receptor fragment of GT1b ganglioside. We also present structural evidence that BKV can utilize glycosaminoglycans as attachment receptors. This work highlights features that underpin capsid stability and provides a platform for rational design and development of urgently needed pharmacological interventions for BKV-associated diseases.

Indexed as

Binding SitesBK VirusCapsid ProteinsCryoelectron MicroscopyCrystallography, X-RayGangliosidesHumansModels, MolecularPolyomavirus InfectionsProtein MultimerizationVirionCapsid ProteinsGangliosidestrisialoganglioside GT1cryo-electron microscopyglycobiologyglycovirologyhuman pathogensmolecular dynamicspolyomaviruspolyomavirus-associated nephropathystructural virologyvirologyvirus-host interactions

Identifiers

PMID29706532
PMCPMC5992339
OpenAlexW2800754876

What OpenQuestion holds

Textmetadata
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.