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Gewählte Publikation:

Hoffmann, D; Mereiter, S; Oh, YJ; Monteil, V; Elder, E; Zhu, R; Canena, D; Hain, L; Laurent, E; Grunwald-Gruber, C; Klausberger, M; Jonsson, G; Kellner, MJ; Novatchkova, M; Ticevic, M; Chabloz, A; Wirnsberger, G; Hagelkruys, A; Altmann, F; Mach, L; Stadlmann, J; Oostenbrink, C; Mirazimi, A; Hinterdorfer, P; Penninger, JM.
(2021): Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites
EMBO J. 2021; 40(19), e108375 FullText FullText_BOKU

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.
Autor*innen der BOKU Wien:
Altmann Friedrich
Grünwald-Gruber Clemens
Klausberger Miriam
Mach Lukas
Oostenbrink Chris
Stadlmann Johannes
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