Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistepbinding of L-fucose to norovirus particles

Alvaro Mallagaray; Christoph Rademacher; Francisco Parra; Grant Hansman; Thomas Peters

doi:10.1093/glycob/cww070

Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistepbinding of L-fucose to norovirus particles

Alvaro Mallagaray, Christoph Rademacher, Francisco Parra, Grant Hansman, Thomas Peters^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Chemie und Metabolomics

16 Zitate (Scopus)

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.

Originalsprache	Englisch
Zeitschrift	Glycobiology
Jahrgang	27
Ausgabenummer	1
Seiten (von - bis)	80-86
Seitenumfang	7
ISSN	0959-6658
DOIs	https://doi.org/10.1093/glycob/cww070
Publikationsstatus	Veröffentlicht - 01.2017

Fördermittel

The German Research Council (DFG) (Grants DFG-PE494/8-1 and DFGPE494/ 12-1 as part of the research unit ViroCarb (FOR 2327) to T.P.). Marie Curie fellowship within the 7th Framework Programme of the EU (Grant Agreement No. 329485, NoroCarb to A.M.). A.M. also thanks the University of Lubeck for financial support. Work at F.P. laboratory has been supported by grant GRUPIN 14-099 from Consejeria de Economia y Empleo of Principado de Asturias and the European Union FEDER program.

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SDG 3 – Gesundheit und Wohlergehen

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Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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10.1093/glycob/cww070

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title = "Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistepbinding of L-fucose to norovirus particles",

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.",

author = "Alvaro Mallagaray and Christoph Rademacher and Francisco Parra and Grant Hansman and Thomas Peters",

note = "Funding Information: The German Research Council (DFG) (Grants DFG-PE494/8-1 and DFGPE494/ 12-1 as part of the research unit ViroCarb (FOR 2327) to T.P.). Marie Curie fellowship within the 7th Framework Programme of the EU (Grant Agreement No. 329485, NoroCarb to A.M.). A.M. also thanks the University of Lubeck for financial support. Work at F.P. laboratory has been supported by grant GRUPIN 14-099 from Consejeria de Economia y Empleo of Principado de Asturias and the European Union FEDER program. Publisher Copyright: {\textcopyright} The Author 2016. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",

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doi = "10.1093/glycob/cww070",

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pages = "80--86",

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T1 - Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistepbinding of L-fucose to norovirus particles

AU - Mallagaray, Alvaro

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AU - Parra, Francisco

AU - Hansman, Grant

AU - Peters, Thomas

N1 - Funding Information: The German Research Council (DFG) (Grants DFG-PE494/8-1 and DFGPE494/ 12-1 as part of the research unit ViroCarb (FOR 2327) to T.P.). Marie Curie fellowship within the 7th Framework Programme of the EU (Grant Agreement No. 329485, NoroCarb to A.M.). A.M. also thanks the University of Lubeck for financial support. Work at F.P. laboratory has been supported by grant GRUPIN 14-099 from Consejeria de Economia y Empleo of Principado de Asturias and the European Union FEDER program. Publisher Copyright: © The Author 2016. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

PY - 2017/1

Y1 - 2017/1

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/85014425426

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JF - Glycobiology

IS - 1

ER -

Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistepbinding of L-fucose to norovirus particles

Abstract

Fördermittel

UN SDGs

Strategische Forschungsbereiche und Zentren

Dokumente

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