| Autor: |
Schütte, Ole M., Patalag, Lukas J., Weber, Lucas M.C., Ries, Annika, Römer, Winfried, Werz, Daniel B., Steinem, Claudia |
| Zdroj: |
Biophysical Journal; June 2015, Vol. 108 Issue: 12 p2775-2778, 4p |
| Abstrakt: |
Shiga toxin subunit B (STxB) binding to its cellular receptor Gb3leads 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-Rfavorably induces large and tightly packed protein clusters, while a lower protein density is found on Gb3-Sdoped membranes. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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