Structural Characterization of N-Linked Glycans in the Receptor Binding Domain of the SARS-CoV-2 Spike Protein and their Interactions with Human Lectins.
Angew Chem Int Ed Engl
; 59(52): 23763-23771, 2020 12 21.
Article
in English
| MEDLINE | ID: covidwho-888056
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 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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Polysaccharides
/
Models, Molecular
/
Lectins, C-Type
/
Spike Glycoprotein, Coronavirus
/
Receptors, Coronavirus
/
Angiotensin-Converting Enzyme 2
/
SARS-CoV-2
Type of study:
Experimental Studies
Limits:
Humans
Language:
English
Journal:
Angew Chem Int Ed Engl
Year:
2020
Document Type:
Article
Affiliation country:
Anie.202011015
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