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Publication Abstract from PubMed

For host colonization, the human fungal pathogen Candida glabrata is known to utilize a large family of highly related surface-exposed cell wall proteins, the lectin-like epithelial adhesins (Epas). To reveal the structure-function relationships within the entire Epa family, we have performed a large-scale functional analysis of the adhesion (A) domains of seventeen Epa paralogs in combination with 3D-structural studies of selected members with cognate ligands. Our study shows that most EpaA domains exert lectin-like functions and together recognize a wide variety of glycans with terminal galactosides for conferring epithelial cell adhesion. We further identify several conserved and variable structural features within the diverse Epa ligand binding pockets, which affect affinity and specificity. These features rationalize why mere phylogenetic relationships within the Epa family are weak indicators for functional classification and explain how Epa-like adhesins have evolved in C. glabrata and related fungal species.

Structural Hotspots Determine Functional Diversity of the Candida glabrata Epithelial Adhesin Family.,Diderrich R, Kock M, Maestre-Reyna M, Keller P, Steuber H, Rupp S, Essen LO, Mosch HU J Biol Chem. 2015 Jun 23. pii: jbc.M115.655654. PMID:26105055^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.