Evidence map›Paper›PMID 41559400›Full record

ArticleNature chemical biology2026

Xylosyltransferase engineering to manipulate proteoglycans in mammalian cells.

Zhen Li, Himanshi Chawla, Lucia Di Vagno, Aisling Ní Cheallaigh, Meg Critcher, Douglas Sammon, Edgar Gonzalez-Rodriguez, David C Briggs, Nara Chung, Vincent Chang and 15 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. ChemBioParis 2025: Approaching Biology Through Chemistry in the City of Light.Chembiochem : a European journal of chemical biology · 2026
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

25 authors.

Zhen Li *Department of Chemistry, Imperial College London, London, UK.
Himanshi Chawla *Department of Chemistry, Imperial College London, London, UK.
Lucia Di VagnoChemical Glycobiology Laboratory, The Francis Crick Institute, London, UK.
Aisling Ní CheallaighLennard-Jones Laboratory, School of Chemical and Physical Sciences and Centre for Glycoscience, Keele University, Keele, UK.
Meg CritcherSkaggs Graduate School of Chemical and Biological Sciences, Scripps Research Institute, La Jolla, CA, USA.ORCID http://orcid.org/0000-0002-3048-4072
Douglas SammonDepartment of Life Sciences, Imperial College London, London, UK.ORCID http://orcid.org/0000-0002-5014-1165
Edgar Gonzalez-RodriguezDepartment of Chemistry, Imperial College London, London, UK.
David C BriggsSignalling and Structural Biology Laboratory, The Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-9793-7339
Nara ChungDepartment of Chemistry, Yale University, New Haven, CT, USA.
Vincent ChangDepartment of Chemistry, Yale University, New Haven, CT, USA.
Keira E MahoneyDepartment of Chemistry, Yale University, New Haven, CT, USA.ORCID http://orcid.org/0000-0003-4561-9838
Anna CioceDepartment of Chemistry, Imperial College London, London, UK.ORCID http://orcid.org/0000-0001-7284-1712
Ganka Bineva-ToddChemical Glycobiology Laboratory, The Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0001-8926-9417
Pei-Ying WangGlycogenetics, Inc., Taipei, Taiwan.
Yi-Chang LiuGlycogenetics, Inc., Taipei, Taiwan.ORCID http://orcid.org/0000-0001-9642-1042
Lloyd D MurphyYork Structural Biology Laboratory and York Biomedical Research Institute, Department of Chemistry, University of York, York, UK.
Yen-Hsi ChenCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.
Yoshiki NarimatsuCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0003-1428-5695
Rebecca L MillerCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0001-8574-1948
Lianne I WillemsYork Structural Biology Laboratory and York Biomedical Research Institute, Department of Chemistry, University of York, York, UK.ORCID http://orcid.org/0000-0001-5411-1329
Stacy A MalakerDepartment of Chemistry, Yale University, New Haven, CT, USA.ORCID http://orcid.org/0000-0003-2382-5067
Mia L HuangSkaggs Graduate School of Chemical and Biological Sciences, Scripps Research Institute, La Jolla, CA, USA.ORCID http://orcid.org/0000-0001-9909-9554
Gavin J MillerLennard-Jones Laboratory, School of Chemical and Physical Sciences and Centre for Glycoscience, Keele University, Keele, UK.
Erhard HohenesterDepartment of Life Sciences, Imperial College London, London, UK.ORCID http://orcid.org/0000-0002-0813-7218
Benjamin SchumannDepartment of Chemistry, Imperial College London, London, UK. benjamin.schumann@tu-dresden.de.ORCID http://orcid.org/0000-0001-5504-0147

Funding

Bridging the Glycome and Proteome with Chemical BiologyR35GM142462 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI Mia L Huang · 2021 to 2026
$2.9M
EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 851448NIGMS NIH HHS R35 GM142462Novo Nordisk Fonden (Novo Nordisk Foundation) NNF22OC0073736RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/T01279X/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/V008439/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EP/T007397/1RCUK | MRC | Medical Research Foundation MR/T019522/1U.S. Department of Health & Human Services | National Institutes of Health (NIH) R35GM142462Wellcome Trust CC2068Wellcome Trust CC2127
6 · The paper itself

Abstract

Mammalian cells receive signaling instructions through interactions on their surfaces. Proteoglycans are critical to these interactions, carrying long glycosaminoglycans that recruit signaling molecules. Biosynthetic redundancy in the first glycosylation step by two xylosyltransferases XT1/2 complicates annotation of proteoglycans. Here we develop a chemical genetic strategy that manipulates the glycan attachment site of cellular proteoglycans. Through a bump-and-hole tactic, we engineer the two isoenzymes XT1 and XT2 to specifically transfer the chemically tagged xylose analog 6AzGlc to target proteins. The tag contains a bioorthogonal functionality, allowing to visualize and profile target proteins in mammalian cells. Unlike xylose analogs, 6AzGlc is amenable to cellular nucleotide-sugar biosynthesis, establishing the XT1/2 bump-and-hole tactic in cells. The approach allows pinpointing glycosylation sites by mass spectrometry and exploiting the chemical handle to manufacture proteoglycans with defined glycosaminoglycan chains for cellular applications. Engineered XT enzymes permit an orthogonal view into proteoglycan biology through conventional techniques in biochemistry.

Indexed as

PentosyltransferasesProtein EngineeringProteoglycansAnimalsGlycosaminoglycansGlycosylationHumansUDP Xylose-Protein XylosyltransferaseXyloseGlycosaminoglycansPentosyltransferasesProteoglycansUDP Xylose-Protein XylosyltransferaseXylose

Identifiers

PMID41559400
PMCPMC13038410

What OpenQuestion holds

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Registered trials

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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.