title: Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistep-binding 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.
authors: Center of Structural and Cell Biology in Medicine, Institute of Chemistry, University of Luebeck, Ratzeburger Allee 160, 23562 Luebeck, Germany.
authors: Alvaro
authors: A
authors: Mallagaray
authors: Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476 Potsdam, Germany.
authors: Christoph
authors: C
authors: Rademacher
authors: Universidad de Oviedo, Instituto Universitario de Biotecnología de Asturias, 33006 Oviedo Spain.
authors: Francisco
authors: F
authors: Parra
authors: Schaller Research Group at the University of Heidelberg and the DKFZ, 69120 Heidelberg, Germany.|Department of Infectious Diseases and Virology, University of Heidelberg, 69120 Heidelberg, Germany.
authors: Grant
authors: G
authors: Hansman
authors: Center of Structural and Cell Biology in Medicine, Institute of Chemistry, University of Luebeck, Ratzeburger Allee 160, 23562 Luebeck, Germany thomas.peters@chemie.uni-luebeck.de.
authors: Thomas
authors: T
authors: Peters
mesh_terms: D001789:Blood Group Antigens / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D036022:Capsid Proteins / Q000737:chemistry* / Q000648:ultrastructure; D018360:Crystallography, X-Ray; D005643:Fucose / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D029322:Norovirus / Q000737:chemistry* / Q000648:ultrastructure; D011485:Protein Binding; D014771:Virion / Q000737:chemistry / Q000648:ultrastructure
chemical_list: D001789:Blood Group Antigens; D036022:Capsid Proteins; D005643:Fucose
keywords: STD NMR titrations; cooperative binding; norovirus infection; protein-carbohydrate interaction; virus-like particles