Evidence map›Paper›PMID 30871026›Full record

ArticleViruses2019

Sulfated Glycosaminoglycans as Viral Decoy Receptors for Human Adenovirus Type 37.

Naresh Chandra, Yan Liu, Jing-Xia Liu, Lars Frängsmyr, Nian Wu, Lisete M Silva, Mona Lindström, Wengang Chai, Fatima Pedrosa Domellöf, Ten Feizi and 1 more

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

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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 2 institutions in 2 countries.

Naresh ChandraSection of Virology, Department of Clinical Microbiology, Umeå University, SE-90185 Umeå, Sweden. naresh.chandra@umu.se.ORCID 0000-0002-8551-3256
Yan LiuGlycosciences Laboratory, Faculty of Medicine, Imperial College of London, Hammersmith Campus, London W12 0NN, UK. yan.liu2@imperial.ac.uk.
Jing-Xia LiuDepartment of Integrative Medical Biology, Umeå University, SE-90185 Umeå, Sweden. jingxia.liu@umu.se.
Lars FrängsmyrSection of Virology, Department of Clinical Microbiology, Umeå University, SE-90185 Umeå, Sweden. lars.frangsmyr@umu.se.
Nian WuGlycosciences Laboratory, Faculty of Medicine, Imperial College of London, Hammersmith Campus, London W12 0NN, UK. n.wu14@imperial.ac.uk.
Lisete M SilvaGlycosciences Laboratory, Faculty of Medicine, Imperial College of London, Hammersmith Campus, London W12 0NN, UK. l.machado-e-silva@imperial.ac.uk.
Mona LindströmDepartment of Integrative Medical Biology, Umeå University, SE-90185 Umeå, Sweden. mona.lindstrom@umu.se.
Wengang ChaiGlycosciences Laboratory, Faculty of Medicine, Imperial College of London, Hammersmith Campus, London W12 0NN, UK. w.chai@imperial.ac.uk.
Fatima Pedrosa DomellöfDepartment of Integrative Medical Biology, Umeå University, SE-90185 Umeå, Sweden. fatima.pedrosa-domellof@umu.se.
Ten FeiziGlycosciences Laboratory, Faculty of Medicine, Imperial College of London, Hammersmith Campus, London W12 0NN, UK. t.feizi@imperial.ac.uk.
Niklas ArnbergSection of Virology, Department of Clinical Microbiology, Umeå University, SE-90185 Umeå, Sweden. niklas.arnberg@umu.se.ORCID 0000-0002-7069-6678
Umeå University · SEHammersmith Hospital · GB

Funding

Wellcome Trust 099197MA
6 · The paper itself

Abstract

Glycans on plasma membranes and in secretions play important roles in infection by many viruses. Species D human adenovirus type 37 (HAdV-D37) is a major cause of epidemic keratoconjunctivitis (EKC) and infects target cells by interacting with sialic acid (SA)-containing glycans via the fiber knob domain of the viral fiber protein. HAdV-D37 also interacts with sulfated glycosaminoglycans (GAGs), but the outcome of this interaction remains unknown. Here, we investigated the molecular requirements of HAdV-D37 fiber knob:GAG interactions using a GAG microarray and demonstrated that fiber knob interacts with a broad range of sulfated GAGs. These interactions were corroborated in cell-based assays and by surface plasmon resonance analysis. Removal of heparan sulfate (HS) and sulfate groups from human corneal epithelial (HCE) cells by heparinase III and sodium chlorate treatments, respectively, reduced HAdV-D37 binding to cells. Remarkably, removal of HS by heparinase III enhanced the virus infection. Our results suggest that interaction of HAdV-D37 with sulfated GAGs in secretions and on plasma membranes prevents/delays the virus binding to SA-containing receptors and inhibits subsequent infection. We also found abundant HS in the basement membrane of the human corneal epithelium, which may act as a barrier to sub-epithelial infection. Collectively, our findings provide novel insights into the role of GAGs as viral decoy receptors and highlight the therapeutic potential of GAGs and/or GAG-mimetics in HAdV-D37 infection.

Indexed as

A549 CellsAdenoviruses, HumanDNA, ViralEpithelium, CornealGenome, ViralGlycosaminoglycansHeparan SulfateHumansMicroarray AnalysisPhylogenyReceptors, VirusViral ProteinsViral TropismVirus AttachmentDNA, ViralGlycosaminoglycansHeparan SulfateReceptors, VirusViral Proteinsadenovirusantiviral drugscellular receptordecoy receptorepidemic keratoconjunctivitisglycosaminoglycantropism

Identifiers

PMID30871026
PMCPMC6466042
OpenAlexW2921898462

What OpenQuestion holds

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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.