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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...

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Hauptverfasser: Mallagaray, Alvaro (VerfasserIn) , Hansman, Grant S. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2017
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
Volltext
Verfasserangaben:Alvaro Mallagaray, Christoph Rademacher, Francisco Parra, Grant Hansman, and Thomas Peters
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 05.09.2018
Advance access publication date: 27 August 2016
Beschreibung:Online Resource
ISSN:1460-2423
DOI:10.1093/glycob/cww070

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