Strengthening relationships: Amyloids create adhesion nanodomains in yeasts

Peter N. Lipke, Melissa C. Garcia, David Alsteens, Caleen B. Ramsook, Stephen A. Klotz, Yves F. Dufrêne

Research output: Contribution to journalReview articlepeer-review

84 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)59-65
Number of pages7
JournalTrends in Microbiology
Issue number2
StatePublished - Feb 2012

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)
  • Infectious Diseases
  • Virology


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