Structural characterization of the N-linked glycans in the receptor binding domain of the SARS-CoV-2 spike protein and*their interactions with human lectins using NMR spectroscopy.
 

Structural characterization of the N-linked glycans in the receptor binding domain of the SARS-CoV-2 spike protein and*their interactions with human lectins using NMR spectroscopy.

Structural characterization of the N-linked glycans in the receptor binding domain of the SARS-CoV-2 spike protein and*their interactions with human lectins using NMR spectroscopy.

Angew Chem Int Ed Engl. 2020 Sep 11;:

Authors: Lenza MP, Oyenarte I, Diercks T, Quintana JI, Gimeno A, Bosch A, Coelho H, Diniz A, Peccati F, Delgado S, Valle M, Millet O, Abrescia NGA, Palazón A, Marcelo F, Jimenez-Oses G, Jimenez-Barbero J, Arda A, Ereño-Orbea J

Abstract
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*13C-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,*15N-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.


PMID: 32915505 [PubMed - as supplied by publisher]



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