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Volume 272, Number 46, Issue of November 14, 1997 pp. 28954-28961
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

KEX2 Influences Candida albicans Proteinase Secretion and Hyphal Formation

(Received for publication, May 7, 1997, and in revised form, August 6, 1997)

George Newport and Nina Agabian ^§¶

From the Departments of  Stomatology, ^§ Pharmaceutical Chemistry, and ^¶ Microbiology & Immunology, University of California at San Francisco, San Francisco, California 94143-0422

Candida albicans possesses at least seven differentially expressed genes that encode virulence-related secretory aspartyl proteinases (Saps). Sap DNA sequences predict post-translational processing at lysine-arginine residues in the preproteins, reminiscent of the maturation of Saccharomyces cerevisiae -factor, where a prepropolypeptide is converted into a biologically active pheromone by Kex2, a subtilisin-like proprotein convertase. To investigate involvement of a C. albicans KEX2 homologue in Sap activation, a genetic selection was performed based on KEX2 function. A kex2 strain of S. cerevisiae was transformed with a C. albicans genomic DNA library and screened for the production of active -factor. Positive clones were assayed for killer toxin activity, another Kex2-dependent phenotype. Plasmids that rescued both defects contained a sequence encoding a protein homologous to S. cerevisiae Kex2. Both alleles of the C. albicans KEX2 were inactivated by successive mutations. Null mutants continued to secrete active Sap2; however, the enzyme was abnormally processed and secreted at reduced levels. Unexpectedly, null mutants were incapable of forming hyphae, instead differentiating into aberrantly shaped cells. The ability to normally process Sap2 and form hyphae was restored upon transformation of null mutants with a KEX2-containing plasmid.

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