2-Hydroxy Fatty Acid Enantiomers of Gb3 Impact Shiga Toxin Binding and Membrane Organization |
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| Authors: | Ole?M. Schütte Lukas?J. Patalag Lucas?M.C. Weber Annika Ries Winfried R?mer Daniel?B. Werz Claudia Steinem |
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| Affiliation: | 1.Institute of Organic and Biomolecular Chemistry, University of Göttingen, Göttingen, Germany;2.Institute of Organic Chemistry, Technical University Braunschweig, Braunschweig, Germany;3.Faculty of Biology and BIOSS-Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany |
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| Abstract: | Shiga toxin subunit B (STxB) binding to its cellular receptor Gb3 leads to the formation of protein-lipid clusters and bending of the membrane. A newly developed synthetic route allowed synthesizing the biologically most relevant Gb3-C24:1 2OH species with both, the natural (Gb3-R) as well as the unnatural (Gb3-S) configuration of the 2OH group. The derivatives bind STxB with identical nanomolar affinity, while the propensity to induce membrane tubules in giant unilamellar vesicles is more pronounced for Gb3-S. Fluorescence and atomic force microscopy images of phase-separated supported membranes revealed differences in the lateral organization of the protein on the membrane. Gb3-R favorably induces large and tightly packed protein clusters, while a lower protein density is found on Gb3-S doped membranes. |
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