Abstract
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.
Highlights
Cellular adhesion is fundamental in many biological processes such as the development of multicellular organisms, as well as in a variety of contexts that are important to the life cycles of unicellular organisms [1,2]
As discussed in this review, only three-dimensional (3D) structures of a few adhesins belonging to three protein families of the yeast species S. cerevisiae, C. albicans and C. glabrata, have been solved
Pfam database mining shows that the structural domains that are present in these solved structures are present in many other fungi, including many pathogenic yeasts, and they appear in various protein architectures
Summary
Cellular adhesion is fundamental in many biological processes such as the development of multicellular organisms, as well as in a variety of contexts that are important to the life cycles of unicellular organisms [1,2]. Many fungi contain a family of cell wall glycoproteins, called “adhesins”, that confer unique adhesion properties [1] These proteins are required for the interactions of fungal cells with each other (flocculation and filamentation) [1] and other cells such as in host–pathogen interactions [2]. The budding yeast Saccharomyces cerevisiae usually grows as a unicellular microorganism, but it can switch to a wide range of multicellular phenotypes, such as flocs, flors, filaments, and biofilms in response to changes in the environment and its genetic background [6] These phenotypes enable S. cerevisiae to colonize various habitats, forage for nutrients, and escape unfavorable conditions [6,7,8,9]. C. glabrata and other non-albicans Candida species are nowadays considered as emerging opportunistic organisms, since they represent an increasing number of fungal infections, which depends on the resistance of these yeasts to several antimicrobial agents [25,26]. S. cerevisiae–lectin–flocculation interaction, cell-cell binding based on S. cerevisiae–Flo11p interaction, C. albicans–Als protein interactions, and C. glabrata–Epa protein interactions
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