Proteolytic cleavage of covalently linked cell wall proteins by Candida albicans Sap9 and Sap10.

ABSTRACT: The cell wall of the human-pathogenic fungus Candida albicans is a robust but also dynamic structure which mediates adaptation to changing environmental conditions during infection. Sap9 and Sap10 are cell surface-associated proteases which function in C. albicans cell wall integrity and interaction with human epithelial cells and neutrophils. In this study, we have analyzed the enzymatic properties of Sap9 and Sap10 and investigated whether these proteases cleave proteins on the fungal cell surface. We show that Sap9 and Sap10, in contrast to other aspartic proteases, exhibit a near-neutral pH optimum of proteolytic activity and prefer the processing of peptides containing basic or dibasic residues. However, both proteases also cleaved at nonbasic sites, and not all tested peptides with d

SUBMITTER: Schild L 

PROVIDER: S-EPMC3019796 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature