• Skip to primary navigation
  • Skip to main content
  • Skip to footer
COVID19-NMR

COVID19-NMR

  • About
    • Mission
    • Participation Guidelines
    • Data Management Plan
    • Research Targets
    • Timeline
  • News
  • Results
    • RNA Results
    • Protein Results
    • Screening RNA
    • Screening Protein
  • Publications
  • Participants
    • Core Team
    • Research Partners
    • Lab Members
    • Corporate Partners
    • Governance Board

Publications

DOI

Angewandte Chemie International Edition (2020) 59:23763 –2377

Structural Characterization of N-Linked Glycans in the Receptor Binding Domain of the SARS-CoV-2 Spike Protein and their Interactions with Human Lectins

M. P. Lenza, I. Oyenarte, T. Diercks, J. I.Quintana, A. Gimeno, H. Coelho, A. Diniz, F. Peccati, S. Delgado, A. Bosch, M. Valle, O. Millet, N. G. A. Abrescia, A. Palazón, F. Marcelo, G. Jiménez‐Osés, J. Jiménez‐Barbero, A. Ardá, J. Ereño‐Orbea

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.

Funded by


Goethe Corona Fonds

DFG

Volkswagen Stiftung

Footer

Coordination

Prof. Dr. Harald Schwalbe (Coordinator)
Institut für Organische Chemie und Chemische Biologie
Zentrum für Biomolekulare Magnetische Resonanz

Johann Wolfgang Goethe-Universität
N160-3.13
Max-von-Laue-Strasse 7
D-60438 Frankfurt am Main

Contact us

++49 69 798 29737
schwalbe@nmr.uni-frankfurt.de

Twitter
 LOGS

Scientific Data Management powered by
Communication powered by
SIGNALS

Imprint | Privacy Policy

This website uses cookies to improve your experience. We'll assume you're ok with this, but you can opt-out if you wish. Cookie settingsACCEPT
Privacy & Cookies Policy

Privacy Overview

This website uses cookies to improve your experience while you navigate through the website. Out of these cookies, the cookies that are categorized as necessary are stored on your browser as they are essential for the working of basic functionalities of the website. We also use third-party cookies that help us analyze and understand how you use this website. These cookies will be stored in your browser only with your consent. You also have the option to opt-out of these cookies. But opting out of some of these cookies may have an effect on your browsing experience.
Necessary
Always Enabled
Necessary cookies are absolutely essential for the website to function properly. This category only includes cookies that ensures basic functionalities and security features of the website. These cookies do not store any personal information.
Non-necessary
Any cookies that may not be particularly necessary for the website to function and is used specifically to collect user personal data via analytics, ads, other embedded contents are termed as non-necessary cookies. It is mandatory to procure user consent prior to running these cookies on your website.
SAVE & ACCEPT