Evidence map›Paper›PMID 25329320›Full record

ArticlePLoS pathogens2014

A sialic acid binding site in a human picornavirus.

Georg Zocher, Nitesh Mistry, Martin Frank, Irmgard Hähnlein-Schick, Jens-Ola Ekström, Niklas Arnberg, Thilo Stehle

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.8field-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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  4. Review
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  8. Article
  9. Synthesis of 4-The Journal of organic chemistry · 2021
    Article
  10. Article
  11. Article
  12. The Role of Glycosylation in Infectious Diseases.Advances in experimental medicine and biology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Virus recognition of glycan receptors.Current opinion in virology · 2019
    Review
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

7 authors at 4 institutions in 3 countries.

Georg ZocherInterfaculty Institute of Biochemistry, University Tübingen, Tübingen, Germany.
Nitesh MistryDivision of Virology, Department of Clinical Microbiology, Umeå University, Umeå, Sweden.
Martin FrankBiognos AB, Göteborg, Sweden.
Irmgard Hähnlein-SchickInterfaculty Institute of Biochemistry, University Tübingen, Tübingen, Germany.
Jens-Ola EkströmDepartment of Molecular Biology, Umeå University, Umeå, Sweden.
Niklas ArnbergDivision of Virology, Department of Clinical Microbiology, Umeå University, Umeå, Sweden; Laboratory for Molecular Infection Medicine (MIMS), Umeå University, Umeå, Sweden.
Thilo StehleInterfaculty Institute of Biochemistry, University Tübingen, Tübingen, Germany; Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee, United States of America.
Umeå University · SEUniversity of Tübingen · DEBiognos (Sweden) · SEVanderbilt University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The picornaviruses coxsackievirus A24 variant (CVA24v) and enterovirus 70 (EV70) cause continued outbreaks and pandemics of acute hemorrhagic conjunctivitis (AHC), a highly contagious eye disease against which neither vaccines nor antiviral drugs are currently available. Moreover, these viruses can cause symptoms in the cornea, upper respiratory tract, and neurological impairments such as acute flaccid paralysis. EV70 and CVA24v are both known to use 5-N-acetylneuraminic acid (Neu5Ac) for cell attachment, thus providing a putative link between the glycan receptor specificity and cell tropism and disease. We report the structures of an intact human picornavirus in complex with a range of glycans terminating in Neu5Ac. We determined the structure of the CVA24v to 1.40 Å resolution, screened different glycans bearing Neu5Ac for CVA24v binding, and structurally characterized interactions with candidate glycan receptors. Biochemical studies verified the relevance of the binding site and demonstrated a preference of CVA24v for α2,6-linked glycans. This preference can be rationalized by molecular dynamics simulations that show that α2,6-linked glycans can establish more contacts with the viral capsid. Our results form an excellent platform for the design of antiviral compounds to prevent AHC.

Indexed as

Binding SitesCell LineEnterovirus C, HumanHumansPicornaviridaeReceptors, VirusSialic AcidsReceptors, VirusSialic Acids

Identifiers

PMID25329320
PMCPMC4199766
OpenAlexW2061648074

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.