title: The conserved PA14 domain of cell wall-associated fungal adhesins governs their glycan-binding specificity.
abstract: Yeast cell wall-associated, lectin-like adhesins form large families that mediate flocculation and host cell recognition. The glycan specificity of individual adhesins is largely unknown. Zupancic et al. (this issue of Molecular Microbiology) used glycan microarrays to compare the glycan-binding characteristics of individual adhesins (Epa proteins) of the pathogenic yeast Candida glabrata produced in the non-adherent yeast Saccharomyces cerevisiae. By sequence swapping between the conserved PA14 domains of two related Epa proteins, they identified a pentapeptide that determines binding specificity and cell adherence and is located on a surface loop of the known crystal structure of the anthrax toxin PA14 domain.
authors.affiliation: Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, 1018 WV, Amsterdam, The Netherlands.
authors.forename: Piet W J
authors.initials: PW
authors.lastname: de Groot
authors.forename: Frans M
authors.initials: FM
authors.lastname: Klis
mesh_terms: D001665:Binding Sites; D041221:Candida glabrata / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D005936:Glucans / Q000378:metabolism*; D017434:Protein Structure, Tertiary
chemical_list: D015815:Cell Adhesion Molecules; D005656:Fungal Proteins; D005936:Glucans