The dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae
Fungal adhesins (Als) or flocculins are family of cell surface proteins that mediate adhesion to diverse biotic and abiotic surfaces. A striking characteristic of Als proteins originally identified in the pathogenic Candida albicans is to form functional amyloids that mediate cis-interaction leading...
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eLife Sciences Publications Ltd
2021
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oai:doaj.org-article:72300f2502d3476f81ad9d88774bf6ce2021-11-25T12:31:46ZThe dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae10.7554/eLife.685922050-084Xe68592https://doaj.org/article/72300f2502d3476f81ad9d88774bf6ce2021-09-01T00:00:00Zhttps://elifesciences.org/articles/68592https://doaj.org/toc/2050-084XFungal adhesins (Als) or flocculins are family of cell surface proteins that mediate adhesion to diverse biotic and abiotic surfaces. A striking characteristic of Als proteins originally identified in the pathogenic Candida albicans is to form functional amyloids that mediate cis-interaction leading to the formation of adhesin nanodomains and trans-interaction between amyloid sequences of opposing cells. In this report, we show that flocculins encoded by FLO11 in Saccharomyces cerevisiae behave like adhesins in C. albicans. To do so, we show that the formation of nanodomains under an external physical force requires a threshold number of amyloid-forming sequences in the Flo11 protein. Then, using a genome editing approach, we constructed strains expressing variants of the Flo11 protein under the endogenous FLO11 promoter, leading to the demonstration that the loss of amyloid-forming sequences strongly reduces cell-cell interaction but has no effect on either plastic adherence or invasive growth in agar, both phenotypes being dependent on the N- and C-terminal ends of Flo11p. Finally, we show that the location of Flo11 is not altered either by the absence of amyloid-forming sequences or by the removal of the N- or C-terminus of the protein.Clara BouyxMarion SchiavoneMarie-Ange TesteEtienne DagueNathalie SieczkowskiAnne JulienJean Marie FrançoiseLife Sciences Publications Ltdarticlecell surfaceamyloidscell adhesionFLO11AFMMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021) |
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DOAJ |
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| topic |
cell surface amyloids cell adhesion FLO11 AFM Medicine R Science Q Biology (General) QH301-705.5 |
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cell surface amyloids cell adhesion FLO11 AFM Medicine R Science Q Biology (General) QH301-705.5 Clara Bouyx Marion Schiavone Marie-Ange Teste Etienne Dague Nathalie Sieczkowski Anne Julien Jean Marie François The dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae |
| description |
Fungal adhesins (Als) or flocculins are family of cell surface proteins that mediate adhesion to diverse biotic and abiotic surfaces. A striking characteristic of Als proteins originally identified in the pathogenic Candida albicans is to form functional amyloids that mediate cis-interaction leading to the formation of adhesin nanodomains and trans-interaction between amyloid sequences of opposing cells. In this report, we show that flocculins encoded by FLO11 in Saccharomyces cerevisiae behave like adhesins in C. albicans. To do so, we show that the formation of nanodomains under an external physical force requires a threshold number of amyloid-forming sequences in the Flo11 protein. Then, using a genome editing approach, we constructed strains expressing variants of the Flo11 protein under the endogenous FLO11 promoter, leading to the demonstration that the loss of amyloid-forming sequences strongly reduces cell-cell interaction but has no effect on either plastic adherence or invasive growth in agar, both phenotypes being dependent on the N- and C-terminal ends of Flo11p. Finally, we show that the location of Flo11 is not altered either by the absence of amyloid-forming sequences or by the removal of the N- or C-terminus of the protein. |
| format |
article |
| author |
Clara Bouyx Marion Schiavone Marie-Ange Teste Etienne Dague Nathalie Sieczkowski Anne Julien Jean Marie François |
| author_facet |
Clara Bouyx Marion Schiavone Marie-Ange Teste Etienne Dague Nathalie Sieczkowski Anne Julien Jean Marie François |
| author_sort |
Clara Bouyx |
| title |
The dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae |
| title_short |
The dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae |
| title_full |
The dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae |
| title_fullStr |
The dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae |
| title_full_unstemmed |
The dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae |
| title_sort |
dual role of amyloid-β-sheet sequences in the cell surface properties of flo11-encoded flocculins in saccharomyces cerevisiae |
| publisher |
eLife Sciences Publications Ltd |
| publishDate |
2021 |
| url |
https://doaj.org/article/72300f2502d3476f81ad9d88774bf6ce |
| work_keys_str_mv |
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1718413502478024704 |