Evidence map›Paper›PMID 25135641›Full record

ArticleThe Journal of biological chemistry2014

Glycomic characterization of respiratory tract tissues of ferrets: implications for its use in influenza virus infection studies.

Nan Jia, Wendy S Barclay, Kim Roberts, Hui-Ling Yen, Renee W Y Chan, Alfred K Y Lam, Gillian Air, J S Malik Peiris, Anne Dell, John M Nicholls and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
4.7field-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

67 citing papers in PubMed, 101 citations in OpenAlex.

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7 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

11 authors at 3 institutions in 3 countries.

Nan JiaFrom the Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Wendy S Barclaythe Faculty of Medicine, Division of Infectious Disease, Imperial College London, Norfolk Place, London W2 1PG, United Kingdom.
Kim Robertsthe Faculty of Medicine, Division of Infectious Disease, Imperial College London, Norfolk Place, London W2 1PG, United Kingdom.
Hui-Ling Yenthe School of Public Health, University of Hong Kong, Pokfulam, Hong Kong SAR, China.
Renee W Y Chanthe School of Public Health, University of Hong Kong, Pokfulam, Hong Kong SAR, China.
Alfred K Y Lamthe Department of Pathology, Griffith University, 4111 Queensland, Australia.
Gillian Airthe Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73126-0901, and.
J S Malik Peiristhe School of Public Health, University of Hong Kong, Pokfulam, Hong Kong SAR, China.
Anne DellFrom the Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
John M Nichollsthe Department of Pathology, University of Hong Kong, Pokfulam, Hong Kong SAR, China nicholls@pathology.hku.hk.
Stuart M HaslamFrom the Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom, s.haslam@imperial.ac.uk.
Imperial College London · GBUniversity of Hong Kong · HKUniversity of Oklahoma Health Sciences Center · US

Funding

Human & mouse antibodies against influenza virusR01AI050933 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI AIR, GILLIAN M · 2003 to 2012
$2.9M
Biotechnology and Biological Sciences Research Council BB/F008309/1Biotechnology and Biological Sciences Research Council BB/K016164/1National Centre for the Replacement, Refinement and Reduction of Animals in Research G1000033/1NIAID NIH HHS R01 AI050933Wellcome TrustWellcome Trust 082098
6 · The paper itself

Abstract

The initial recognition between influenza virus and the host cell is mediated by interactions between the viral surface protein hemagglutinin and sialic acid-terminated glycoconjugates on the host cell surface. The sialic acid residues can be linked to the adjacent monosaccharide by α2-3- or α2-6-type glycosidic bonds. It is this linkage difference that primarily defines the species barrier of the influenza virus infection with α2-3 binding being associated with avian influenza viruses and α2-6 binding being associated with human strains. The ferret has been extensively used as an animal model to study the transmission of influenza. To better understand the validity of this model system, we undertook glycomic characterization of respiratory tissues of ferret, which allows a comparison of potential viral receptors to be made between humans and ferrets. To complement the structural analysis, lectin staining experiments were performed to characterize the regional distributions of glycans along the respiratory tract of ferrets. Finally, the binding between the glycans identified and the hemagglutinins of different strains of influenza viruses was assessed by glycan array experiments. Our data indicated that the respiratory tissues of ferret heterogeneously express both α2-3- and α2-6-linked sialic acids. However, the respiratory tissues of ferret also expressed the Sda epitope (NeuAcα2-3(GalNAcβ1-4)Galβ1-4GlcNAc) and sialylated N,N'-diacetyllactosamine (NeuAcα2-6GalNAcβ1-4GlcNAc), which have not been observed in the human respiratory tract surface epithelium. The presence of the Sda epitope reduces potential binding sites for avian viruses and thus may have implications for the usefulness of the ferret in the study of influenza virus infection.

Indexed as

GlycomicsAnimalsBinding SitesCarbohydrate SequenceDisease Models, AnimalFemaleFerretsHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A virusLectinsMaleMolecular Sequence DataOrthomyxoviridae InfectionsPolysaccharidesProtein BindingHemagglutinin Glycoproteins, Influenza VirusLectinsPolysaccharidesSialic AcidsCarbohydrate StructureGlycomicsInfluenza VirusMass Spectrometry (MS)Sialic Acid

Identifiers

PMID25135641
PMCPMC4192499
OpenAlexW2093083195

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.