Dehydration of model membranes induced by lectins from Ricinus communis and Viscum album.

The effects of ribosome-inactivating proteins (RIPs) from Ricinus communis and from Viscum album on the water permeability, Pf, and the surface dielectric constant, epsilon, of model membranes were studied. Pf was calculated from microelectrode measurements of the ion concentration distribution in the immediate vicinity of a planar membrane, and epsilon was obtained from the fluorescence of dansyl phosphatidylethanolamine incorporated into unilamellar vesicles. Pf and epsilon of fully saturated phosphatidylcholine membranes were affected only in the presence of a lectin receptor (monosialoganglioside, GM1) in the bilayer. It is suggested that the membrane area occupied by clustered lectin-receptor complexes is markedly less permeable to water. Protein binding to the receptor was not a prelude for hydrophobic lipid-protein interactions when the membranes were formed from a mixture of natural phospholipids with a high content of unsaturated fatty acids. These membranes, characterized by a high initial water permeability, were found to interact with the RIPs unspecifically. From a decrease of both Pf and epsilon it was concluded that not only water partitioning but also protein adsorption correlates with looser packing of polyunsaturated lipids at the lipid-water interface.

Membrane fusion mediated by ricin and viscumin.

The ribosome inactivating plant proteins (RIPs) ricin and viscumin but not Ricinus communis agglutinin are able induce vesicle-vesicle fusion. A model is suggested in which the toxicity of the RIPs is partially determined by their fusogenicity. Herein, fusion is hypothesized to allow the RIPs to leak across endocytic vesicles to approve their access to cytoplasmic ribosomes.