TY - JOUR
T1 - Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistepbinding of L-fucose to norovirus particles
AU - Mallagaray, Alvaro
AU - Rademacher, Christoph
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 - http://www.scopus.com/inward/record.url?scp=85014425426&partnerID=8YFLogxK
U2 - 10.1093/glycob/cww070
DO - 10.1093/glycob/cww070
M3 - Journal articles
C2 - 27496762
AN - SCOPUS:85014425426
SN - 0959-6658
VL - 27
SP - 80
EP - 86
JO - Glycobiology
JF - Glycobiology
IS - 1
ER -
