The Physically Driven Invagination of Lectins in Glycolipid Containing Giant Unilamellar Vesicles.
A masterpiece of synthetic glycobiology describes how the rational design of neolectins having engineered glycolipid binding sites provides an unambiguous proof of the invagination of carbohydrate binding proteins in giant unilamellar vesicles. Neolectins have been designed with controlled number and position of binding sites to decipher the role of multivalency on avidity to a glycosylated surface and on membrane dynamics of glycolipids. Whereas the presence of at least two binding sites is required for avidity to occur, the ability to bend and invaginate membranes is critically dependent on the distance between two adjacent binding sites.
There does exist a physical process by which membrane glycosphingolipids trigger the internalization of bacterial and plant toxins and viruses through glycan binding. A likely hypothesis regarding the energy at origin of this physical process would be the line tension generated by the formation of glycolipid domains resulting in negative membrane curvature and formation of membrane invagination.