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Cell Press, Trends in Microbiology, 2(20), p. 59-65, 2012

DOI: 10.1016/j.tim.2011.10.002

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Strengthening relationships: amyloids create adhesion nanodomains in yeasts

Journal article published in 2011 by Peter N. Lipke, Melissa C. Garcia, David Alsteens ORCID, Caleen B. Ramsook, Stephen A. Klotz, Yves F. Dufrêne
This paper is available in a repository.
This paper is available in a repository.

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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.