4.8 Article

Membrane Deformation by Neolectins with Engineered Glycolipid Binding Sites

期刊

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 53, 期 35, 页码 9267-9270

出版社

WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201404568

关键词

lectms; hposomes; membranes; multivalency; oligosaccharides

资金

  1. Agence Nationale de la Recherche Grant NeoLect [ANR-11-BSV5-002]
  2. CNRS
  3. Universite Grenoble Alpes
  4. Excellence Initiative of the German Research Foundation [EXC 294]
  5. Ministry of Science, Research and the Arts of Baden-Wurttemberg [Az: 33-7532.20]
  6. European Research Council [ERC-2011-StG 282105]
  7. COST actions [CM1102, BM1003]
  8. Labex ARCANE [ANR-11-LABX-003]

向作者/读者索取更多资源

Lectins are glycan-binding proteins that are involved in the recognition of glycoconju gates 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.

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