Nestor, Gustav
- Department of Molecular Sciences, Swedish University of Agricultural Sciences
- University of Pittsburgh
Abstract
Cyanovirin-N (CV-N) is a cyanobacterial lectin with antiviral activity towards HIV and several other viruses. Here, we identify mannoside hydroxyl protons that are hydrogen bonded to the protein backbone of the CV-N domain B binding site, using NMR spectroscopy. For the two carbohydrate ligands Manα(1→2)ManαOMe and Manα(1→2) Manα(1→6)ManαOMe five hydroxyl protons are involved in hydrogen-bonding networks. Comparison with previous crystallographic results revealed that four of these hydroxyl protons donate hydrogen bonds to protein backbone carbonyl oxygens in solution and in the crystal. Hydrogen bonds were not detected between the side chains of Glu41 and Arg76 with sugar hydroxyls, as previously proposed for CV-N binding of mannosides. Molecular dynamics simulations of the CV-N/Manα(1→2)Manα(1→6)ManαOMe complex confirmed the NMR-determined hydrogen-bonding network. Detailed characterization of CV-N/mannoside complexes provides a better understanding of lectin-carbohydrate interactions and opens up to the use of CV-N and similar lectins as antiviral agents.
Keywords
carbohydrates; cyanovirin-N; hydrogen bonds; hydroxyls; NMR spectroscopy
Published in
Glycobiology
2021, volume: 31, number: 4, pages: 508-518
SLU Authors
UKÄ Subject classification
Structural Biology
Publication identifier
- DOI: https://doi.org/10.1093/glycob/cwaa081
Permanent link to this page (URI)
https://res.slu.se/id/publ/112183