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

David Hoffmann, View ORCID ProfileStefan Mereiter, View ORCID ProfileYoo Jin Oh, Vanessa Monteil, Rong Zhu, Daniel Canena, Lisa Hain, Elisabeth Laurent, Clemens Grünwald-Gruber, Maria Novatchkova, Melita Ticevic, Antoine Chabloz, Gerald Wirnsberger, Astrid Hagelkruys, Friedrich Altmann, View ORCID ProfileLukas Mach, Johannes Stadlmann, Chris Oostenbrink, View ORCID ProfileAli Mirazimi, Peter Hinterdorfer, View ORCID ProfileJosef M. Penninger
doi: https://doi.org/10.1101/2021.04.01.438087
David Hoffmann
1IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences; 1030, Vienna; Austria
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Stefan Mereiter
1IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences; 1030, Vienna; Austria
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Yoo Jin Oh
2Institute of Biophysics, Johannes Kepler University Linz, Gruberstr. 40, 4020 Linz, Austria
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Vanessa Monteil
3Karolinska Institute and Karolinska University Hospital, Department of Laboratory Medicine, Unit of Clinical Microbiology, 17177 Stockholm, Sweden
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Rong Zhu
2Institute of Biophysics, Johannes Kepler University Linz, Gruberstr. 40, 4020 Linz, Austria
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Daniel Canena
2Institute of Biophysics, Johannes Kepler University Linz, Gruberstr. 40, 4020 Linz, Austria
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Lisa Hain
2Institute of Biophysics, Johannes Kepler University Linz, Gruberstr. 40, 4020 Linz, Austria
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Elisabeth Laurent
4Department of Biotechnology and BOKU Core Facility Biomolecular & Cellular Analysis, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria
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Clemens Grünwald-Gruber
5Department of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
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Maria Novatchkova
1IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences; 1030, Vienna; Austria
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Melita Ticevic
1IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences; 1030, Vienna; Austria
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Antoine Chabloz
6Department of Medical Genetics, Life Science Institute, University of British Columbia, Vancouver, Canada
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Gerald Wirnsberger
7Apeiron Biologics, Campus Vienna Biocenter 5, 1030 Vienna, Austria
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Astrid Hagelkruys
1IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences; 1030, Vienna; Austria
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Friedrich Altmann
5Department of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
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Lukas Mach
8Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
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Johannes Stadlmann
1IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences; 1030, Vienna; Austria
5Department of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
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Chris Oostenbrink
9Institute for Molecular Modeling and Simulation, Department for Material Sciences and Process Engineering, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
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Ali Mirazimi
3Karolinska Institute and Karolinska University Hospital, Department of Laboratory Medicine, Unit of Clinical Microbiology, 17177 Stockholm, Sweden
10National Veterinary Institute, 751 89 Uppsala, Sweden
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Peter Hinterdorfer
2Institute of Biophysics, Johannes Kepler University Linz, Gruberstr. 40, 4020 Linz, Austria
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Josef M. Penninger
1IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences; 1030, Vienna; Austria
6Department of Medical Genetics, Life Science Institute, University of British Columbia, Vancouver, Canada
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  • For correspondence: josef.penninger@ubc.ca
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Abstract

New SARS-CoV-2 variants are continuously emerging with critical implications for therapies or vaccinations. All 22 N-glycan sites of SARS-CoV-2 Spike remain highly conserved among the variants B.1.1.7, 501Y.V2 and P.1, 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.

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Posted April 01, 2021.
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Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites
David Hoffmann, Stefan Mereiter, Yoo Jin Oh, Vanessa Monteil, Rong Zhu, Daniel Canena, Lisa Hain, Elisabeth Laurent, Clemens Grünwald-Gruber, Maria Novatchkova, Melita Ticevic, Antoine Chabloz, Gerald Wirnsberger, Astrid Hagelkruys, Friedrich Altmann, Lukas Mach, Johannes Stadlmann, Chris Oostenbrink, Ali Mirazimi, Peter Hinterdorfer, Josef M. Penninger
bioRxiv 2021.04.01.438087; doi: https://doi.org/10.1101/2021.04.01.438087
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Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites
David Hoffmann, Stefan Mereiter, Yoo Jin Oh, Vanessa Monteil, Rong Zhu, Daniel Canena, Lisa Hain, Elisabeth Laurent, Clemens Grünwald-Gruber, Maria Novatchkova, Melita Ticevic, Antoine Chabloz, Gerald Wirnsberger, Astrid Hagelkruys, Friedrich Altmann, Lukas Mach, Johannes Stadlmann, Chris Oostenbrink, Ali Mirazimi, Peter Hinterdorfer, Josef M. Penninger
bioRxiv 2021.04.01.438087; doi: https://doi.org/10.1101/2021.04.01.438087

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