Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistep-binding of l-fucose to norovirus particles
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 tha...
Gespeichert in:
| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2017
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| In: |
Glycobiology
Year: 2016, Jahrgang: 27, Heft: 1, Pages: 80-86 |
| ISSN: | 1460-2423 |
| DOI: | 10.1093/glycob/cww070 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1093/glycob/cww070 Verlag, kostenfrei, Volltext: https://academic.oup.com/glycob/article/27/1/80/2528015 
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| Verfasserangaben: | Alvaro Mallagaray, Christoph Rademacher, Francisco Parra, Grant Hansman, and Thomas Peters |
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| 520 | |a 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. | ||
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