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Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Sweet entanglements--protein:glycan interactions in two HIV-inactivating lectin families
Leonardus M I Koharudin1, Angela M Gronenborn
1Department of Structural Biology, School of Medicine, University of Pittsburgh, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA. mik44@pitt.edu
Abstract:
Structures and sugar binding by members of two lectin families, Cyanovirin-N homolog (CVNH) and Oscillatoria Agardhii agglutinin homolog (OAAH), were determined to elucidate the basis for recognition of high-mannose glycans on the HIV envelope glycoprotein gp120. We solved NMR solution and/or crystal structures for several lectins and delineated their carbohydrate specificity by array screening and direct NMR titrations. Both families recognize different epitopes on high-mannose glycans, namely, Manα(1-2)Man units at the end of the D1 and D3 arms and α3,α6-mannopentaose at the central branch point of Man-8 or Man-9 for CVNH and OAAH lectins, respectively.
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