Evidence map›Paper›PMID 24789779›Full record

ArticleJournal of virology2014

A small molecule inhibits virion attachment to heparan sulfate- or sialic acid-containing glycans.

Che C Colpitts, Luis M Schang

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.6field-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

68 citing papers in PubMed, 149 citations in OpenAlex.

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  12. Dual action of epigallocatechin-3-gallate in virus-induced cell Injury.Journal, genetic engineering & biotechnology · 2023
    Article
  13. Article
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  15. Therapeutic potential of green tea catechin, (-)-epigallocatechin-3-Phytomedicine plus : international journal of phytotherapy and phytopharmacology · 2023
    Review
  16. Article
  17. Review
  18. Article
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  20. Article

8 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Che C ColpittsLi Ka Shing Institute of Virology, University of Alberta, Edmonton, AB, Canada Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB, Canada.
Luis M SchangDepartment of Biochemistry, University of Alberta, Edmonton, AB, Canada Li Ka Shing Institute of Virology, University of Alberta, Edmonton, AB, Canada Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB, Canada luis.schang@ualberta.ca.
University of Alberta · CA

Funding

Canadian Institutes of Health Research MOP 13033
6 · The paper itself

Abstract

Primary attachment to cellular glycans is a critical entry step for most human viruses. Some viruses, such as herpes simplex virus type 1 (HSV-1) and hepatitis C virus (HCV), bind to heparan sulfate, whereas others, such as influenza A virus (IAV), bind to sialic acid. Receptor mimetics that interfere with these interactions are active against viruses that bind to either heparan sulfate or to sialic acid. However, no molecule that inhibits the attachment of viruses in both groups has yet been identified. Epigallocatechin gallate (EGCG), a green tea catechin, is active against many unrelated viruses, including several that bind to heparan sulfate or to sialic acid. We sought to identify the basis for the broad-spectrum activity of EGCG. Here, we show that EGCG inhibits the infectivity of a diverse group of enveloped and nonenveloped human viruses. EGCG acts directly on the virions, without affecting the fluidity or integrity of the virion envelopes. Instead, EGCG interacts with virion surface proteins to inhibit the attachment of HSV-1, HCV, IAV, vaccinia virus, adenovirus, reovirus, and vesicular stomatitis virus (VSV) virions. We further show that EGCG competes with heparan sulfate for binding of HSV-1 and HCV virions and with sialic acid for binding of IAV virions. Therefore, EGCG inhibits unrelated viruses by a common mechanism. Most importantly, we have identified EGCG as the first broad-spectrum attachment inhibitor. Our results open the possibility for the development of small molecule broad-spectrum antivirals targeting virion attachment. Importance: This study shows that it is possible to develop a small molecule antiviral or microbicide active against the two largest groups of human viruses: those that bind to glycosaminoglycans and those that bind to sialoglycans. This group includes the vast majority of human viruses, including herpes simplex viruses, cytomegalovirus, influenza virus, poxvirus, hepatitis C virus, HIV, and many others.

Indexed as

AnimalsAntiviral AgentsCatechinChlorocebus aethiopsDNA VirusesDogsHeparan SulfateMadin Darby Canine Kidney CellsN-Acetylneuraminic AcidPolysaccharidesRNA VirusesVero CellsVirionVirus AttachmentAntiviral AgentsCatechinepigallocatechin gallateHeparan SulfateN-Acetylneuraminic AcidPolysaccharides

Identifiers

PMID24789779
PMCPMC4097786
OpenAlexW2126952890

What OpenQuestion holds

Textmetadata
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.