Evidence map›Paper›PMID 42469202›Full record

ArticleNature communications2026

Versatile Glycan Probes for Multiplatform Investigation of Glycan Interactions with Proteins, Viruses, and Cells.

Jin Yu, Alexiane Decout, Jiayun Yang, Antonio Di Maio, Wengang Chai, W Bruce Turnbull, Thilo Stehle, Steven H Sacks, Thomas P Peacock, Munir Iqbal and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Jin YuGlycosciences Laboratory, Department of Metabolism, Digestion and Reproduction, Faculty of Medicine, Imperial College London, London, UK.
Alexiane DecoutInstitute of Reproductive and Developmental Biology, Department of Metabolism, Digestion and Reproduction, Imperial College London, London, UK.ORCID http://orcid.org/0000-0001-7761-6434
Jiayun YangThe Pirbright Institute, Woking, UK.
Antonio Di MaioGlycosciences Laboratory, Department of Metabolism, Digestion and Reproduction, Faculty of Medicine, Imperial College London, London, UK.ORCID http://orcid.org/0000-0002-2740-9098
Wengang ChaiGlycosciences Laboratory, Department of Metabolism, Digestion and Reproduction, Faculty of Medicine, Imperial College London, London, UK.ORCID http://orcid.org/0000-0003-2977-5347
W Bruce TurnbullSchool of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.ORCID http://orcid.org/0000-0002-7352-0360
Thilo StehleInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID http://orcid.org/0000-0002-4571-8548
Steven H SacksMedical Research Council (MRC) Centre for Transplantation, King's College London, London, UK.
Thomas P PeacockThe Pirbright Institute, Woking, UK.ORCID http://orcid.org/0000-0001-7077-2928
Munir IqbalThe Pirbright Institute, Woking, UK.ORCID http://orcid.org/0000-0001-5165-5339
Ten FeiziGlycosciences Laboratory, Department of Metabolism, Digestion and Reproduction, Faculty of Medicine, Imperial College London, London, UK.ORCID http://orcid.org/0000-0001-6495-0329
Yan LiuGlycosciences Laboratory, Department of Metabolism, Digestion and Reproduction, Faculty of Medicine, Imperial College London, London, UK. yan.liu2@imperial.ac.uk.ORCID http://orcid.org/0000-0002-2566-6867

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) FOR2327 ViroCarbMarch of Dimes Foundation (March of Dimes) 22-FY18-82RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BBS/E/PI/230002A; BBS/E/PI/230002B; BBS/E/PI/23NB0003RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/Y007298/1RCUK | Medical Research Council (MRC) MR/R010757/1RCUK | Medical Research Council (MRC) MR/Y03368X/1Wellcome TrustWellcome Trust (Wellcome) WT099197/Z/12/Z, 108430/Z/15/Z, 218304/Z/19ZWellcome Trust (Wellcome) WT218304/Z/19/Z, 108430/Z/15/Z
6 · The paper itself

Abstract

Glycan-mediated interactions are vital to development, microbial colonisation, immune signalling, and cancer progression. Glycan microarrays have revolutionised glycobiology by enabling high-throughput analysis of these complex interactions, supported by techniques that reveal kinetics and dynamics in solution or at the cellular level. We introduce multifunctional glycan probes based on a tri-functional Fmoc-Amino-Azido (FAA) linker, enabling multi-platform investigation of glycan-mediated interactions. These FAA probes support glycan presentation on both covalent and non-covalent array platforms, allowing direct comparison of glycan recognition by diverse proteins. Notably, certain viral adhesins and immune lectins show a preference for the non-covalent platform. The azido group allows further functionalisation via 'click chemistry', enabling biotinylation for immobilisation on bio-layer interferometry biosensors for influenza virus binding, or fluorescent tagging for flow cytometry analysis of glycan-lectin interactions on cells. These versatile probes offer a unified platform for in-depth interrogation of glycan interactions using complementary approaches, with strong potential to advance glycan-based diagnostics and therapeutics.

Indexed as

Molecular ProbesPolysaccharidesProteinsAnimalsAzidesBiosensing TechniquesClick ChemistryFlow CytometryGlycomicsHumansLectinsMicroarray AnalysisAzidesLectinsMolecular ProbesPolysaccharidesProteins

Identifiers

PMID42469202
PMCPMC13493820

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.