Shiga Toxin Induces Lipid Compression: A Mechanism for Generating Membrane Curvature
journal contributionposted on 25.09.2019, 13:34 by Erik B. Watkins, Jaroslaw Majewski, Eva Y. Chi, Haifei Gao, Jean-Claude Florent, Ludger Johannes
Biomembranes are hard to compress laterally, and membrane area compressibility has not been associated with biological processes. Using X-ray surface scattering, we observed that bacterial Shiga toxin compresses lipid packing in a gel phase monolayer upon binding to its cellular receptor, the glycolipid Gb3. This toxin-induced reorganization of lipid packing reached beyond the immediate membrane patch that the protein was bound to, and linkers separating the Gb3 carbohydrate and ceramide moieties modulated the toxin’s capacity to compress the membrane. Within a natural membrane, asymmetric compression of the toxin-bound leaflet could provide a mechanism to initiate narrow membrane bending, as observed upon toxin entry into cells. Such lipid compression and long-range membrane reorganization by glycolipid-binding proteins represent novel concepts in membrane biology that have direct implications for the construction of endocytic pits in clathrin-independent endocytosis.
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membrane area compressibilitymembrane patchShiga toxin compresses lipidmembrane biologyGenerating Membrane Curvature Biomembranesmembrane reorganizationglycolipid-binding proteinsgel phase monolayertoxin-induced reorganizationclathrin-independent endocytosisglycolipid Gb 3.Gb 3 carbohydrateendocytic pitsX-ray surfaceSuch lipid compressiontoxin entryShiga Toxin Induces Lipid Compressionceramide moietiesnovel conceptstoxin-bound leaflet