title: Human immunodeficiency virus type 1 protease inhibitor attenuates Candida albicans virulence properties in vitro.
abstract: The putative virulence factor secreted aspartyl proteinase (SAP) of Candida albicans and the human immunodeficiency virus type 1 (HIV-1) protease both belong to the aspartyl proteinase family. The present study demonstrates that the HIV-1 protease inhibitor Indinavir is a weak but specific inhibitor of SAP. In addition, Indinavir reduces the amount of cell bound as well as released SAP antigen from C. albicans. Furthermore, viability and growth of C. albicans are markedly reduced by Indinavir. These findings indicate that HIV-1 protease inhibitors may possess antifungal activity and we speculate that in vivo SAP inhibition may add to the resolution of mucosal candidiasis in HIV-1 infected subjects.
authors.affiliation: Ludwig Boltzmann-Institut für AIDS-Forschung and Institut für Hygiene, University of Innsbruck, Austria. agruber@ucsd.edu
authors.forename: A
authors.initials: A
authors.lastname: Gruber
authors.forename: C
authors.initials: C
authors.lastname: Speth
authors.forename: E
authors.initials: E
authors.lastname: Lukasser-Vogl
authors.forename: R
authors.initials: R
authors.lastname: Zangerle
authors.forename: M
authors.initials: M
authors.lastname: Borg-von Zepelin
authors.forename: M P
authors.initials: MP
authors.lastname: Dierich
authors.forename: R
authors.initials: R
authors.lastname: Würzner
mesh_terms: D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D002176:Candida albicans / Q000187:drug effects* / Q000201:enzymology / Q000472:pathogenicity; D016333:HIV Protease / Q000187:drug effects*; D017320:HIV Protease Inhibitors / Q000494:pharmacology*; D019469:Indinavir / Q000494:pharmacology*; D008969:Molecular Sequence Data; D014774:Virulence
chemical_list: D017320:HIV Protease Inhibitors; D019469:Indinavir; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease