Strengthening relationships: amyloids create adhesion nanodomains in yeasts

Trends Microbiol. 2012 Feb;20(2):59-65. doi: 10.1016/j.tim.2011.10.002. Epub 2011 Nov 16.

Abstract

Budding yeasts adhere to biotic or abiotic surfaces and aggregate to form biofilms, using wall-anchored glycoprotein adhesins. The process is paradoxical: adhesins often show weak binding to specific ligands, yet mediate remarkably strong adherence. Single-molecule atomic force microscopy (AFM), genomics, biochemistry and cell biology have recently explained the puzzle, with Candida albicans Als adhesins as the paradigm. The strength of adhesion results partly from force-activated amyloid-like clustering of hundreds of adhesin molecules to form arrays of ordered multimeric binding sites. The various protein domains of eukaryotic adhesins cooperate to facilitate this fascinating new mechanism of activation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry
  • Amyloid / metabolism*
  • Binding Sites
  • Biofilms / growth & development*
  • Candida albicans / physiology*
  • Cell Adhesion / physiology
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / metabolism*
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • Microscopy, Atomic Force
  • Molecular Sequence Data
  • Oligosaccharides / metabolism
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Saccharomyces cerevisiae / physiology*

Substances

  • (6-O-aminoethylphosphonato-mannopyranosyl)-(1-2)-mannopyranosyl-(1-6)-mannopyranosyl-(1-4)-(2-amino-2-deoxyglucopyranosyl)-(1-6)-1-O-(1,2-di-O-octadecanoyl-sn-glyceryl-phosphonato)-myo-inositol
  • ALA1 protein, Candida albicans
  • Amyloid
  • Cell Adhesion Molecules
  • Fungal Proteins
  • Oligosaccharides