AFM investigation of Pseudomonas aeruginosa lectin LecA (PA-IL) filaments induced by multivalent glycoclusters

Chem Commun (Camb). 2011 Sep 7;47(33):9483-5. doi: 10.1039/c1cc13097h. Epub 2011 Jul 25.

Abstract

Atomic force microscopy reveals that Pseudomonas aeruginosa LecA (PA-IL) and a tetra-galactosylated 1,3-alternate calix[4]arene-based glycocluster self-assemble according to an aggregative chelate binding mode to create monodimensional filaments. Lectin oligomers are identified along the filaments and defects in chelate binding generate branches and bifurcations. A molecular model with alternate 90° orientation of LecA tetramers is proposed to describe the organisation of lectins and glycoclusters in the filaments.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Binding Sites
  • Calixarenes / chemistry
  • Glycosylation
  • Microscopy, Atomic Force
  • Phenols / chemistry
  • Pseudomonas aeruginosa / metabolism*

Substances

  • Adhesins, Bacterial
  • LecA protein, bacteria
  • Phenols
  • calix(4)arene
  • Calixarenes