Taxonomic distribution of proteins containing Candida_ALS_N domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Candida_ALS_N domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Molecular phylogenetics of ascomycotal adhesins--a novel family ofputative cell-surface adhesive proteins in fission yeasts.

Linder T, Gustafsson CM
Fungal Genet Biol. 2008; 45: 485-97

In this work, we identify a family of putative adhesins in the fissionyeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. Themembers of this family share a conserved tandem repeat related to thosefound in the Candida albicans Als family of adhesins. Unlike previouslycharacterised adhesins that possess conserved ligand-binding domains atthe N-terminus, this group of proteins carry ligand-binding domains attheir C-termini. We demonstrate that one such domain--the uncharacterisedGLEYA domain, is related to the lectin-like ligand-binding domain found inthe Saccharomyces cerevisiae Flo proteins. Unlike the Flo and Alsproteins, the fission yeast adhesins do not contain detectable glycosylphosphatidyl inositol (GPI) membrane anchor signals to mediate theirattachment to the cell wall, which may suggest a novel cell wallattachment mechanism. Further sequence analysis identified severalputative adhesins in the sub-phylum of Pezizomycotina, where only a fewadhesins have been described to date.

A biochemical guide to yeast adhesins: glycoproteins for social andantisocial occasions.

Dranginis AM, Rauceo JM, Coronado JE, Lipke PN
Microbiol Mol Biol Rev. 2007; 71: 282-94

Fungi are nonmotile eukaryotes that rely on their adhesins for selectiveinteraction with the environment and with other fungal cells.Glycosylphosphatidylinositol (GPI)-cross-linked adhesins have essentialroles in mating, colony morphology, host-pathogen interactions, andbiofilm formation. We review the structure and binding properties of cellwall-bound adhesins of ascomycetous yeasts and relate them to theireffects on cellular interactions, with particular emphasis on theagglutinins and flocculins of Saccharomyces and the Als proteins ofCandida. These glycoproteins share common structural motifs tailored tosurface activity and biological function. After being secreted to theouter face of the plasma membrane, they are covalently anchored in thewall through modified GPI anchors, with their binding domains elevatedbeyond the wall surface on highly glycosylated extended stalks. N-terminalglobular domains bind peptide or sugar ligands, with between millimolarand nanomolar affinities. These affinities and the high density ofadhesins and ligands at the cell surface determine microscopic andmacroscopic characteristics of cell-cell associations. Central domainsoften include Thr-rich tandemly repeated sequences that are highlyglycosylated. These domains potentiate cell-to-cell binding, but themolecular mechanism of such an association is not yet clear. These repeatsalso mediate recombination between repeats and between genes. The highlevels of recombination and epigenetic regulation are sources of variationwhich enable the population to continually exploit new niches andresources.