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Structural Characterization of N‐Linked Glycans in the Receptor Binding Domain of the SARS‐CoV‐2 Spike Protein and their Interactions with Human Lectins
Author(s) -
Lenza Maria Pia,
Oyenarte Iker,
Diercks Tammo,
Quintana Jon Imanol,
Gimeno Ana,
Coelho Helena,
Diniz Ana,
Peccati Francesca,
Delgado Sandra,
Bosch Alexandre,
Valle Mikel,
Millet Oscar,
Abrescia Nicola G. A.,
Palazón Asís,
Marcelo Filipa,
JiménezOsés Gonzalo,
JiménezBarbero Jesús,
Ardá Ana,
EreñoOrbea June
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202011015
Subject(s) - galectin , glycan , epitope , glycoprotein , lectin , receptor , chemistry , computational biology , siglec , plasma protein binding , microbiology and biotechnology , biochemistry , biology , antibody , genetics
The glycan structures of the receptor binding domain of the SARS‐CoV2 spike glycoprotein expressed in human HEK293F cells have been studied by using NMR. The different possible interacting epitopes have been deeply analysed and characterized, providing evidence of the presence of glycan structures not found in previous MS‐based analyses. The interaction of the RBD 13 C‐labelled glycans with different human lectins, which are expressed in different organs and tissues that may be affected during the infection process, has also been evaluated by NMR. In particular, 15 N‐labelled galectins (galectins‐3, ‐7 and ‐8 N‐terminal), Siglecs (Siglec‐8, Siglec‐10), and C‐type lectins (DC‐SIGN, MGL) have been employed. Complementary experiments from the glycoprotein perspective or from the lectin's point of view have permitted to disentangle the specific interacting epitopes in each case. Based on these findings, 3D models of the interacting complexes have been proposed.