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Publication Abstract from PubMed

Candida glabrata is an opportunistic pathogenic yeast frequently causing infections in humans. Though it lacks typical virulence factors such as hyphal development, C. glabrata contains a remarkably large and diverse set of putative wall adhesins that is crucial for its success as pathogen. Here, we present an analysis of putative adhesins from the homology clusters V and VI. First, sequence similarity network analysis revealed relationships between cluster V and VI adhesins and S. cerevisiae haze protective factors (Hpf). Crystal structures of A-regions from cluster VI adhesins Awp1 and Awp3b reveal a parallel right-handed beta-helix domain that is linked to a C-terminal beta-sandwich. Structure solution of the A-region of Awp3b via single wavelength anomalous diffraction phasing revealed the largest known lanthanide cluster with 21 Gd3+ ions. Awp1-A and Awp3b-A show structural similarity to pectate lyases but binding to neither carbohydrates nor Ca2+ was observed. Phenotypic analysis of awp1Delta, awp3Delta, and awp1,3Delta double mutants did also not confirm their role as adhesins. In contrast, deletion mutants of the cluster V adhesin Awp2 in the hyperadhesive clinical isolate PEU382 demonstrated its importance for adhesion to polystyrene or glass, biofilm formation, cell aggregation and other cell surface-related phenotypes. Together with cluster III and VII adhesins our study shows that C. glabrata CBS138 can rely on a set of 42 Awp1-related adhesins with beta-helix/alpha-crystallin domain architecture for modifying the surface characteristics of its cell wall.

A novel class of Candida glabrata cell wall proteins with beta-helix fold mediates adhesion in clinical isolates.,Reithofer V, Fernandez-Pereira J, Alvarado M, de Groot P, Essen LO PLoS Pathog. 2021 Dec 28;17(12):e1009980. doi: 10.1371/journal.ppat.1009980., eCollection 2021 Dec. PMID:34962966^[1]

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