Switching of bacterial adhesion to a glycosylated surface by reversible reorientation of the carbohydrate ligand

Angew Chem Int Ed Engl. 2014 Dec 22;53(52):14583-6. doi: 10.1002/anie.201409808. Epub 2014 Nov 27.

Abstract

The surface recognition in many biological systems is guided by the interaction of carbohydrate-specific proteins (lectins) with carbohydrate epitopes (ligands) located within the unordered glycoconjugate layer (glycocalyx) of cells. Thus, for recognition, the respective ligand has to reorient for a successful matching event. Herein, we present for the first time a model system, in which only the orientation of the ligand is altered in a controlled manner without changing the recognition quality of the ligand itself. The key for this orientational control is the embedding into an interfacial system and the use of a photoswitchable mechanical joint, such as azobenzene.

Keywords: azobenzene; carbohydrate recognition; glycocalyx; lectin; light-induced switching.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Escherichia coli / chemistry
  • Adhesins, Escherichia coli / metabolism
  • Azo Compounds / chemistry
  • Bacterial Adhesion
  • Carbohydrates / chemistry*
  • Escherichia coli / physiology
  • Fimbriae Proteins / chemistry
  • Fimbriae Proteins / metabolism
  • Glycosylation
  • Lectins / chemistry*
  • Lectins / metabolism
  • Ligands
  • Mannosides / chemistry
  • Spectrophotometry, Infrared

Substances

  • Adhesins, Escherichia coli
  • Azo Compounds
  • Carbohydrates
  • Lectins
  • Ligands
  • Mannosides
  • fimH protein, E coli
  • Fimbriae Proteins
  • azobenzene