Year: 2012
Journal: Angewandte Chemie Volume 124, Issue 48, pages 12186–12190, November 26, 2012, 20130119
Authors: Marta Bally 1 *, Gustaf E. Rydell 3, Raphael Zahn 5, Waqas Nasir 2, Christian Eggeling 6, Michael E. Breimer 4, Lennart Svensson 7, Fredrik Höök 1, Göran Larson 2 *
Last authors: Göran Larson
Organizations: 1
Department of Applied Physics, Chalmers University of Technology, SE-41133 Göteborg (Sweden) 2
Department of Clinical Chemistry and Transfusion Medicine, Sahlgrenska Academy, University of Gothenburg (Sweden) 3
Traffic, Signaling, and Delivery Laboratory, Centre de Recherche, Institut Curie, CNRS UMR144 (France) 4
Department of Surgery, Sahlgrenska Academy, University of Gothenburg (Sweden) 5
Laboratory of Biosensors and Bioelectronics, Institute of Biomedical Engineering, Universität Zürich und ETH Zürich (Switzerland) 6
Max-Planck-Institut für Biophysikalische Chemie (Germany), Currently: WIMM, University of Oxford (UK) 7
Division of Molecular Virology, University of Linköping (Sweden) Email: Marta Bally (bally@chalmers.se), Göran Larson (goran.larson@clinchem.gu.se) *Department of Applied Physics, Chalmers University of Technology, SE-41133 Göteborg (Sweden) †
The work was supported by grants from the Swedish Research Council (8266 to G.L.), (2010-878 to G.E.R.), Vinnova (F.H., G.L.), and the Swiss National Science Foundation (M.B.). The monospecies galactosylceramides were a gift from Prof. Jan-Eric Månsson, University of Gothenburg.
Country: sverige, Sweden, Gremany, Switzerland
A sticky situation: Domain-dependent recognition of the glycosphingolipid galactosylceramide by norovirus-like particles (see picture; red/yellow) is shown using supported lipid bilayers (purple) as model membranes. Optimal ligand presentation is found to promote strong binding to GalCer. This presentation can be found at the edges of the glycosphingolipid-enriched domains (green) and binding is repressed in the absence of these domains.
