Evidence map›Paper›PMID 34375000›Full record

ArticleThe EMBO journal2021

Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites.

David Hoffmann, Stefan Mereiter, Yoo Jin Oh, Vanessa Monteil, Elizabeth Elder, Rong Zhu, Daniel Canena, Lisa Hain, Elisabeth Laurent, Clemens Grünwald-Gruber and 15 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.8field-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

51 citing papers in PubMed, 76 citations in OpenAlex.

  1. Switching Spike Plasticity Shapes ACE2 Engagement Across SARS-CoV-2 Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Review
  4. Host Glycan-Lectin Interplay in SARS-CoV-2 Infection.International journal of molecular sciences · 2026
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

25 authors at 8 institutions in 3 countries.

David HoffmannIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.
Stefan MereiterIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.ORCID 0000-0002-4832-3090
Yoo Jin OhInstitute of Biophysics, Johannes Kepler University Linz, Linz, Austria.ORCID 0000-0002-9636-3329
Vanessa MonteilDepartment of Laboratory Medicine, Unit of Clinical Microbiology, Karolinska Institute and Karolinska University Hospital, Stockholm, Sweden.ORCID 0000-0002-2652-5695
Elizabeth ElderPublic Health Agency of Sweden, Solna, Sweden.ORCID 0000-0003-1615-2642
Rong ZhuInstitute of Biophysics, Johannes Kepler University Linz, Linz, Austria.
Daniel CanenaInstitute of Biophysics, Johannes Kepler University Linz, Linz, Austria.
Lisa HainInstitute of Biophysics, Johannes Kepler University Linz, Linz, Austria.
Elisabeth LaurentDepartment of Biotechnology and BOKU Core Facility Biomolecular & Cellular Analysis, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0002-5234-5524
Clemens Grünwald-GruberDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Miriam KlausbergerDepartment of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0001-8409-454X
Gustav JonssonIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.ORCID 0000-0001-6692-8395
Max J KellnerIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.
Maria NovatchkovaIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.
Melita TicevicIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.
Antoine ChablozDepartment of Medical Genetics, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada.
Gerald WirnsbergerApeiron Biologics, Vienna, Austria.
Astrid HagelkruysIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.ORCID 0000-0003-3015-4038
Friedrich AltmannDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Lukas MachDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0001-9013-5408
Johannes StadlmannIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.
Chris OostenbrinkDepartment for Material Sciences and Process Engineering, Institute for Molecular Modeling and Simulation, University of Natural Resources and Life Sciences, Vienna, Austria.
Ali MirazimiDepartment of Laboratory Medicine, Unit of Clinical Microbiology, Karolinska Institute and Karolinska University Hospital, Stockholm, Sweden.ORCID 0000-0003-2371-6055
Peter HinterdorferInstitute of Biophysics, Johannes Kepler University Linz, Linz, Austria.ORCID 0000-0003-2583-1305
Josef M PenningerIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria.ORCID 0000-0002-8194-3777
Institute of Molecular Biotechnology · ATBOKU University · ATJohannes Kepler University of Linz · ATApeiron Biologics (Austria) · ATKarolinska University Hospital · SEPublic Health Agency of Sweden · SESwedish Veterinary Agency · SEUniversity of British Columbia · CA

Funding

Austrian Science Fund FWF I 3173Austrian Science Fund FWF P 31599Austrian Science Fund FWF V 584
6 · The paper itself

Abstract

New SARS-CoV-2 variants are continuously emerging with critical implications for therapies or vaccinations. The 22 N-glycan sites of Spike remain highly conserved among SARS-CoV-2 variants, opening an avenue for robust therapeutic intervention. Here we used a comprehensive library of mammalian carbohydrate-binding proteins (lectins) to probe critical sugar residues on the full-length trimeric Spike and the receptor binding domain (RBD) of SARS-CoV-2. Two lectins, Clec4g and CD209c, were identified to strongly bind to Spike. Clec4g and CD209c binding to Spike was dissected and visualized in real time and at single-molecule resolution using atomic force microscopy. 3D modelling showed that both lectins can bind to a glycan within the RBD-ACE2 interface and thus interferes with Spike binding to cell surfaces. Importantly, Clec4g and CD209c significantly reduced SARS-CoV-2 infections. These data report the first extensive map and 3D structural modelling of lectin-Spike interactions and uncovers candidate receptors involved in Spike binding and SARS-CoV-2 infections. The capacity of CLEC4G and mCD209c lectins to block SARS-CoV-2 viral entry holds promise for pan-variant therapeutic interventions.

Indexed as

AnimalsBinding SitesCell LineChlorocebus aethiopsCOVID-19GlycosylationHEK293 CellsHumansMiceMolecular Dynamics SimulationProtein BindingReceptors, MitogenSARS-CoV-2Vero CellsVirus InternalizationReceptors, MitogenglycosylationlectinSARS-CoV-2spike

Identifiers

PMID34375000
PMCPMC8420505
OpenAlexW3193082551

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.