Evidence map›Paper›PMID 24130487›Full record

ArticlePLoS pathogens2013

A structure-guided mutation in the major capsid protein retargets BK polyomavirus.

Ursula Neu, Stacy-Ann A Allen, Bärbel S Blaum, Yan Liu, Martin Frank, Angelina S Palma, Luisa J Ströh, Ten Feizi, Thomas Peters, Walter J Atwood and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.5field-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

58 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
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  7. Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
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  12. Article
  13. Characterization of a glycan-binding complex of minor pilins completes the analysis ofProceedings of the National Academy of Sciences of the United States of America · 2023
    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

11 authors at 6 institutions in 4 countries.

Ursula NeuInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Stacy-Ann A Allen
Bärbel S Blaum
Yan Liu
Martin Frank
Angelina S Palma
Luisa J Ströh
Ten Feizi
Thomas Peters
Walter J Atwood
Thilo Stehle
Imperial College London · GBUniversity of Tübingen · DEBrown University · USBiognos (Sweden) · SEUniversity of Lübeck · DEVanderbilt University · US

Funding

SYNTHETIC CHEMISTRY COREP01NS065719 · NINDS · BROWN UNIVERSITY · PI ATWOOD, WALTER J · 2009 to 2018
$12.3M
Cellular Receptors for the Human PolyomavirusesR01CA071878 · NCI · BROWN UNIVERSITY · PI ATWOOD, WALTER J · 2002 to 2011
$2.6M
NCI NIH HHS 5R01CA71878-13NCI NIH HHS R01 CA071878NINDS NIH HHS P01 NS065719NINDS NIH HHS P01-NS065719Wellcome TrustWellcome Trust WT093378MAWellcome Trust WT099197MA
6 · The paper itself

Abstract

Viruses within a family often vary in their cellular tropism and pathogenicity. In many cases, these variations are due to viruses switching their specificity from one cell surface receptor to another. The structural requirements that underlie such receptor switching are not well understood especially for carbohydrate-binding viruses, as methods capable of structure-specificity studies are only relatively recently being developed for carbohydrates. We have characterized the receptor specificity, structure and infectivity of the human polyomavirus BKPyV, the causative agent of polyomavirus-associated nephropathy, and uncover a molecular switch for binding different carbohydrate receptors. We show that the b-series gangliosides GD3, GD2, GD1b and GT1b all can serve as receptors for BKPyV. The crystal structure of the BKPyV capsid protein VP1 in complex with GD3 reveals contacts with two sialic acid moieties in the receptor, providing a basis for the observed specificity. Comparison with the structure of simian virus 40 (SV40) VP1 bound to ganglioside GM1 identifies the amino acid at position 68 as a determinant of specificity. Mutation of this residue from lysine in BKPyV to serine in SV40 switches the receptor specificity of BKPyV from GD3 to GM1 both in vitro and in cell culture. Our findings highlight the plasticity of viral receptor binding sites and form a template to retarget viruses to different receptors and cell types.

Indexed as

MutationBK VirusCapsid ProteinsGangliosidesHEK293 CellsHumansPolyomavirus InfectionsProtein Structure, TertiaryReceptors, VirusSimian virus 40Capsid ProteinsGangliosidesReceptors, Virus

Identifiers

PMID24130487
PMCPMC3795024
OpenAlexW2019881727

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.