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Adhesins of Yeasts: Protein Structure and Interactions

The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast Saccharomyces cerevisiae can switch from a unicellular lifestyle to a multicellular one. A crucial step in multicellular lifestyle adaptation is self-recognition, self-interaction, and adh...

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Detalles Bibliográficos
Autor principal: Willaert, Ronnie G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6308950/
https://www.ncbi.nlm.nih.gov/pubmed/30373267
http://dx.doi.org/10.3390/jof4040119
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author Willaert, Ronnie G.
author_facet Willaert, Ronnie G.
author_sort Willaert, Ronnie G.
collection PubMed
description The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast Saccharomyces cerevisiae can switch from a unicellular lifestyle to a multicellular one. A crucial step in multicellular lifestyle adaptation is self-recognition, self-interaction, and adhesion to abiotic surfaces. Infectious yeast diseases such as candidiasis are initiated by the adhesion of the yeast cells to host cells. Adhesion is accomplished by adhesin proteins that are attached to the cell wall and stick out to interact with other cells or substrates. Protein structures give detailed insights into the molecular mechanism of adhesin-ligand interaction. Currently, only the structures of a very limited number of N-terminal adhesion domains of adhesins have been solved. Therefore, this review focuses on these adhesin protein families. The protein architectures, protein structures, and ligand interactions of the flocculation protein family of S. cerevisiae; the epithelial adhesion family of C. glabrata; and the agglutinin-like sequence protein family of C. albicans are reviewed and discussed.
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spelling pubmed-63089502019-06-17 Adhesins of Yeasts: Protein Structure and Interactions Willaert, Ronnie G. J Fungi (Basel) Review The ability of yeast cells to adhere to other cells or substrates is crucial for many yeasts. The budding yeast Saccharomyces cerevisiae can switch from a unicellular lifestyle to a multicellular one. A crucial step in multicellular lifestyle adaptation is self-recognition, self-interaction, and adhesion to abiotic surfaces. Infectious yeast diseases such as candidiasis are initiated by the adhesion of the yeast cells to host cells. Adhesion is accomplished by adhesin proteins that are attached to the cell wall and stick out to interact with other cells or substrates. Protein structures give detailed insights into the molecular mechanism of adhesin-ligand interaction. Currently, only the structures of a very limited number of N-terminal adhesion domains of adhesins have been solved. Therefore, this review focuses on these adhesin protein families. The protein architectures, protein structures, and ligand interactions of the flocculation protein family of S. cerevisiae; the epithelial adhesion family of C. glabrata; and the agglutinin-like sequence protein family of C. albicans are reviewed and discussed. MDPI 2018-10-27 /pmc/articles/PMC6308950/ /pubmed/30373267 http://dx.doi.org/10.3390/jof4040119 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Willaert, Ronnie G.
Adhesins of Yeasts: Protein Structure and Interactions
title Adhesins of Yeasts: Protein Structure and Interactions
title_full Adhesins of Yeasts: Protein Structure and Interactions
title_fullStr Adhesins of Yeasts: Protein Structure and Interactions
title_full_unstemmed Adhesins of Yeasts: Protein Structure and Interactions
title_short Adhesins of Yeasts: Protein Structure and Interactions
title_sort adhesins of yeasts: protein structure and interactions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6308950/
https://www.ncbi.nlm.nih.gov/pubmed/30373267
http://dx.doi.org/10.3390/jof4040119
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