期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 52, 页码 23763-23771出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202011015
关键词
glycan; lectin; molecular recognition; receptor binding domain; SARS-CoV2
资金
- European Research Council (ERC-2017-AdG) [788143-RECGLYCANMR]
- Mizutani Foundation for Glycoscience [200077]
- Agencia Estatal Investigacion of Spain (AEI) [RTI2018-094751-B-C21, RTI2018-095700-B-I00, PGC2018-098996-B-I00, RTI2018-099592-B-C22, RTI2018-101269-B-I00]
- Agencia Estatal Investigacion of Spain (AEI
- Ramon y Cajal)
- Severo Ochoa Excellence Accreditation [SEV-2016-0644]
- FundacAo para a Ciencia e a Tecnologia (Portugal) [IF/00780/2015, PTDC/BIA-MIB/31028/2017, UCIBIO UIDB/04378/2020, 22161, PD/BD/142847/2018]
- Fundação para a Ciência e a Tecnologia [PTDC/BIA-MIB/31028/2017, PD/BD/142847/2018] Funding Source: FCT
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 (RBDC)-C-13-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,N-15-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.
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