Abstract
Selective adhesion of fungal cells to one another and to foreign surfaces is fundamental for the development of multicellular growth forms and the successful colonization of substrates and host organisms. Accordingly, fungi possess diverse cell wall-associated adhesins, mostly large glycoproteins, which present N-terminal adhesion domains at the cell surface for ligand recognition and binding. In order to function as robust adhesins, these glycoproteins must be covalently linkedto the cell wall via C-terminal glycosylphosphatidylinositol (GPI) anchors by transglycosylation. In this review, we summarize the current knowledge on the structural and functional diversity of so far characterized protein families of adhesion domains and set it into a broad context by an in-depth bioinformatics analysis using sequence similarity networks. In addition, we discuss possible mechanisms for the membrane-to-cell wall transfer of fungal adhesins by membrane-anchored Dfg5 transglycosidases.
Highlights
In fungi, selective cell adhesion is fundamental for numerous biological processes including multicellularCell wall-associated proteins (CWPs) are usually polysaccharide-linked glycoproteins, which fulfil a plethora of functions including adhesion, absorption of molecules, signal transduction and protection as well as synthesis and reorganization of wall components and anchoring of cell wall proteins (Bowman and Free 2006)
We summarize the current knowledge on the structural and functional diversity of so far characterized protein families of adhesion domains and set it into a broad context by an in-depth bioinformatics analysis using sequence similarity networks
Comparative genomic analysis has revealed that the number of genes for GPI-CWP adhesins present in different fungal species can be highly variable ranging from less than 10, as exemplified by the budding yeast Saccharomyces cerevisiae (Brückner and Mösch 2012) or non-pathogenic Candida species (Gabaldon et al 2013), to much higher numbers as found for the most frequently isolated human fungal pathogens Candida albicans or Candida glabrata that contains more than 80 members (Timmermans et al 2018; Xu et al 2020)
Summary
Selective cell adhesion is fundamental for numerous biological processes including multicellularCell wall-associated proteins (CWPs) are usually polysaccharide-linked glycoproteins, which fulfil a plethora of functions including adhesion, absorption of molecules, signal transduction and protection as well as synthesis and reorganization of wall components and anchoring of cell wall proteins (Bowman and Free 2006). Functional in vivo and in vitro analysis has been performed on more than 20 different PA14-type GPI-CWPs revealing that their N-terminal A domains are lectins that confer cell-cell and cell-substrate adhesion by specific binding of diverse glycan ligands in a C-type lectin-like manner.
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