Evidence map›Paper›PMID 33893239›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Probing the binding specificities of human Siglecs by cell-based glycan arrays.

Christian Büll, Rebecca Nason, Lingbo Sun, Julie Van Coillie, Daniel Madriz Sørensen, Sam J Moons, Zhang Yang, Steven Arbitman, Steve M Fernandes, Sanae Furukawa and 8 more

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

120 citing papers in PubMed, 174 citations in OpenAlex.

  1. Sialic acidOncoimmunology · 2026
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  9. Defining substrate specificities ofOrganic chemistry frontiers : an international journal of organic chemistry · 2026
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60 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

18 authors at 4 institutions in 3 countries.

Christian BüllCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.ORCID 0000-0001-7785-2920
Rebecca NasonCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Lingbo SunCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Julie Van CoillieCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Daniel Madriz SørensenCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.ORCID 0000-0001-8811-2506
Sam J MoonsCluster for Molecular Chemistry, Institute for Molecules and Materials, Radboud University Nijmegen, 6525 AJ Nijmegen, The Netherlands.ORCID 0000-0001-5507-3811
Zhang YangCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Steven ArbitmanDepartment of Pharmacology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.ORCID 0000-0001-5839-0193
Steve M FernandesDepartment of Pharmacology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.ORCID 0000-0002-5677-916X
Sanae FurukawaCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Ryan McBrideDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037.
Corwin M NycholatDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037.
Gosse J AdemaDepartment of Radiation Oncology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, 6525 GA Nijmegen, The Netherlands.
James C PaulsonDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037.
Ronald L SchnaarDepartment of Pharmacology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.ORCID 0000-0002-7701-5484
Thomas J BoltjeCluster for Molecular Chemistry, Institute for Molecules and Materials, Radboud University Nijmegen, 6525 AJ Nijmegen, The Netherlands.ORCID 0000-0001-9141-8784
Henrik ClausenCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark; hclau@sund.ku.dk yoshiki@sund.ku.dk.ORCID 0000-0002-0915-5055
Yoshiki NarimatsuCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark; hclau@sund.ku.dk yoshiki@sund.ku.dk.ORCID 0000-0003-1428-5695
University of Copenhagen · DKJohns Hopkins University · USRadboud University Nijmegen · NLScripps Research Institute · US

Funding

Treating lung inflammation by targeting SiglecsP01HL107151 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI SCHNAAR, RONALD L · 2011 to 2017
$15.4M
Using siglecs and their ligands to treat allergic diseases SALTADU19AI136443 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BOCHNER, BRUCE S · 2018 to 2022
$7.6M
NHLBI NIH HHS P01 HL107151NIAID NIH HHS U19 AI136443
6 · The paper itself

Abstract

Siglecs are a family of sialic acid-binding receptors expressed by cells of the immune system and a few other cell types capable of modulating immune cell functions upon recognition of sialoglycan ligands. While human Siglecs primarily bind to sialic acid residues on diverse types of glycoproteins and glycolipids that constitute the sialome, their fine binding specificities for elaborated complex glycan structures and the contribution of the glycoconjugate and protein context for recognition of sialoglycans at the cell surface are not fully elucidated. Here, we generated a library of isogenic human HEK293 cells with combinatorial loss/gain of individual sialyltransferase genes and the introduction of sulfotransferases for display of the human sialome and to dissect Siglec interactions in the natural context of glycoconjugates at the cell surface. We found that Siglec-4/7/15 all have distinct binding preferences for sialylated GalNAc-type O-glycans but exhibit selectivity for patterns of O-glycans as presented on distinct protein sequences. We discovered that the sulfotransferase CHST1 drives sialoglycan binding of Siglec-3/8/7/15 and that sulfation can impact the preferences for binding to O-glycan patterns. In particular, the branched Neu5Acα2-3(6-

Indexed as

Gene Knockout TechniquesHEK293 CellsHumansMucin-1PolysaccharidesSialic Acid Binding Immunoglobulin-like LectinsSialyltransferasesTissue Array AnalysisMucin-1PolysaccharidesSialic Acid Binding Immunoglobulin-like LectinsSialyltransferasesCD33cell-based glycan arraysialomesialyltransferaseSiglecs

Identifiers

PMID33893239
PMCPMC8092401
OpenAlexW3155392711

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.