Journal article

STD NMR spectroscopy and molecular modeling investigation of the binding of N-acetylneuraminic acid derivatives to rhesus rotavirus VP8*core

Thomas Haselhorst, Helen Blanchard, Martin Frank, Mark J Kraschnefski, Milton J Kiefel, Alex J Szyczew, Jeffery C Dyason, Fiona Fleming, Gavan Holloway, Barbara S Coulson, Mark von Itzstein

GLYCOBIOLOGY | OXFORD UNIV PRESS INC | Published : 2007

Abstract

The VP8* subunit of rotavirus spike protein VP4 contains a sialic acid (Sia)-binding domain important for host cell attachment and infection. In this study, the binding epitope of the N-acetylneuraminic acid (Neu5Ac) derivatives has been characterized by saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy. From this STD NMR data, it is proposed that the VP8* core recognizes an identical binding epitope in both methyl alpha-D-N-acetylneuraminide (Neu5Acalpha2Me) and the disaccharide methyl S-(alpha-D-N-acetylneuraminosyl)-(2-->6)-6-thio-beta-D-galactopyranoside (Neu5Ac-alpha(2,6)-S-Galbeta1Me). In the VP8*-disaccharide complex, the Neu5Ac moiety contributes to t..

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University of Melbourne Researchers