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Shiga Toxin Induces Lipid Compression: A Mechanism for Generating Membrane Curvature.
Nano Lett 2019; 19(10):7365-7369NL

Abstract

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.

Authors+Show Affiliations

MPA-11: Materials Synthesis and Integrated Devices , Los Alamos National Laboratory , Los Alamos , New Mexico 87545 , United States.Theoretical Biology and Biophysics , Los Alamos National Laboratory , Los Alamos , New Mexico 87545 , United States. Division of Molecular and Cellular Biosciences , National Science Foundation , Alexandria , Virginia 22314 , United States. Department of Chemical and Biological Engineering and the Center for Biomedical Engineering , University of New Mexico , Albuquerque , New Mexico 87131 , United States.Department of Chemical and Biological Engineering and the Center for Biomedical Engineering , University of New Mexico , Albuquerque , New Mexico 87131 , United States.Cellular and Chemical Biology Unit , Institut Curie, PSL Research University , U1143 INSERM, UMR3666 CNRS , 26 rue d'Ulm , 75248 Paris Cedex 05, France.Cellular and Chemical Biology Unit , Institut Curie, PSL Research University , U1143 INSERM, UMR3666 CNRS , 26 rue d'Ulm , 75248 Paris Cedex 05, France.Cellular and Chemical Biology Unit , Institut Curie, PSL Research University , U1143 INSERM, UMR3666 CNRS , 26 rue d'Ulm , 75248 Paris Cedex 05, France.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31538793

Citation

Watkins, Erik B., et al. "Shiga Toxin Induces Lipid Compression: a Mechanism for Generating Membrane Curvature." Nano Letters, vol. 19, no. 10, 2019, pp. 7365-7369.
Watkins EB, Majewski J, Chi EY, et al. Shiga Toxin Induces Lipid Compression: A Mechanism for Generating Membrane Curvature. Nano Lett. 2019;19(10):7365-7369.
Watkins, E. B., Majewski, J., Chi, E. Y., Gao, H., Florent, J. C., & Johannes, L. (2019). Shiga Toxin Induces Lipid Compression: A Mechanism for Generating Membrane Curvature. Nano Letters, 19(10), pp. 7365-7369. doi:10.1021/acs.nanolett.9b03001.
Watkins EB, et al. Shiga Toxin Induces Lipid Compression: a Mechanism for Generating Membrane Curvature. Nano Lett. 2019 Oct 9;19(10):7365-7369. PubMed PMID: 31538793.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Shiga Toxin Induces Lipid Compression: A Mechanism for Generating Membrane Curvature. AU - Watkins,Erik B, AU - Majewski,Jaroslaw, AU - Chi,Eva Y, AU - Gao,Haifei, AU - Florent,Jean-Claude, AU - Johannes,Ludger, Y1 - 2019/09/25/ PY - 2019/9/21/pubmed PY - 2019/9/21/medline PY - 2019/9/21/entrez KW - Biomembrane KW - Shiga toxin KW - endocytosis KW - membrane curvature SP - 7365 EP - 7369 JF - Nano letters JO - Nano Lett. VL - 19 IS - 10 N2 - 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. SN - 1530-6992 UR - https://www.unboundmedicine.com/medline/citation/31538793/Shiga_toxin_induces_lipid_compression:_a_mechanism_for_generating_membrane_curvature L2 - https://dx.doi.org/10.1021/acs.nanolett.9b03001 DB - PRIME DP - Unbound Medicine ER -