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Membrane Deformation by Neolectins with Engineered Glycolipid Binding Sites
Author(s) -
Arnaud Julie,
Tröndle Kevin,
Claudi Julie,
Audfray Aymeric,
Varrot Annabelle,
Römer Winfried,
Imberty Anne
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201404568
Subject(s) - glycolipid , avidity , lectin , glycoconjugate , membrane , chemistry , fucose , glycan , biophysics , biochemistry , binding site , plasma protein binding , glycoprotein , biology , antibody , immunology
Lectins are glycan‐binding proteins that are involved in the recognition of glycoconjugates at the cell surface. When binding to glycolipids, multivalent lectins can affect their distribution and alter membrane shapes. Neolectins have now 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. A monomeric hexavalent neolectin has been first engineered from a trimeric hexavalent bacterial lectin, From this neolectin template, 13 different neolectins with a valency ranging from 0 to 6 were designed, produced, and analyzed for their ability to bind fucose in solution, to attach to a glycosylated surface and to invaginate glycolipid‐containing giant liposomes. Whereas the avidity only depends on the presence of at least two binding sites, the ability to bend and invaginate membranes critically depends on the distance between two adjacent binding sites.