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- Title
Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistepbinding of L-fucose to norovirus particles.
- Authors
Mallagaray, Alvaro; Rademacher, Christoph; Parra, Francisco; Hansman, Grant; Peters, Thomas
- Abstract
Recently, combined nuclear magnetic resonance (NMR), native mass spectrometry (MS) and X-ray crystallographic studies have demonstrated that binding of histo-blood group antigens (HBGAs) to norovirus capsid protein (P-dimers) is a cooperative process involving four binding pockets. Here, we show that binding to norovirus virus-like particles (VLPs) is even more complex. We performed saturation transfer difference (STD) NMR titration experiments with two representative genotypes of norovirus VLPs using L-fucose as a minimal HBGA. Compared to titrations with P-dimers, the corresponding binding isotherms reflect at least six distinct binding events.
- Subjects
MAGNETIZATION transfer; FUCOSE; NUCLEAR magnetic resonance; NOROVIRUSES; BLOOD group antigens
- Publication
Glycobiology, 2017, Vol 27, Issue 1, p80
- ISSN
0959-6658
- Publication type
Article
- DOI
10.1093/glycob/cww070