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, 20 (2), 59-65

Strengthening Relationships: Amyloids Create Adhesion Nanodomains in Yeasts

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Strengthening Relationships: Amyloids Create Adhesion Nanodomains in Yeasts

Peter N Lipke et al. Trends Microbiol.

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.

Figures

Figure 1
Figure 1
Als proteins: multidomain adhesion proteins that form amyloids. (a) Model illustrating the domains of Als protein. (b) Model showing how homotypic binding of Als adhesins and mechanical stimulus lead to formation of cell surface amyloid nanodomains activating cell adhesion.
Figure 2
Figure 2
Induction of surface nanodomains follows application of extending force to individual Als molecules on the surface of yeasts. On the left are AFM images of yeast trapped in a microporous membrane. The second column shows maps of position of Als proteins within the 1 μm square marked “1=1’.” Blue pixels show interactions of <150 pN and red pixels show interactions resistant to forces >150 pN. Clusters of 10 or more contiguous colored pixels are outlined in white [13]. The third column shows clustering of the Als molecules in a second mapping of the same region of the cell walls, and the last column shows similar clustering in a remote region (Map 2). Clustering is a result of surface amyloid formation, as shown by lack of clustering in cells expressing the non-amyloid V326N form of Als5p. Reprinted with permission from Garcia et al. [13].
Figure 3
Figure 3
Confocal imaging of amyloid patches on aggregated C. albicans Day 286. These are activated in a cell adhesion assay and stained with thioflavin T, 100 nM. (a) and (d) aggregated cells. (b) Fluorescence was enhanced after incubation with an amyloid-promoting peptide from Als5p. (c) Anti-amyloid V326N peptide inhibits aggregation and extinguishes fluorescence [13]. (d) Regions of enhanced fluorescence are marked where cells are tightly apposed. Bars represent 8 μm. Reprinted with permission from Garcia et al. [13].

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