title: Aspartyl proteinases of Candida albicans and their role in pathogenicity.
abstract: Among the putative virulence factors of Candida albicans, secreted aspartic proteinases (Sap, encoded by a family of at least nine genes) continue to attract the attention of many investigators studying the pathogenesis of candidiasis. Several early studies documented a correlation between the levels of Sap secretion and the virulence of different strains, but much stronger support for this role has been provided by more recent data on differential SAP gene(s) expression in ex vivo and in vivo models, the outcome of infections with SAP-deleted mutants, and use of Sap immunogens. In particular, some SAP-deleted strains suffered a substantial loss of virulence, and, more interestingly, this was specifically associated with selected gene products and selected experimental pathologies. Moreover, anti-Sap antibodies have been shown to mediate a degree of protection in an experimental, mucosal candidiasis model. There is now initial evidence that distinct Saps are differentially produced in various Candida illnesses or stages of them. The exact mechanisms of each Sap involvement in any particular Candida disease, with special regard to human infections, and how the immune system deals with Sap, are critical issues for future research. An answer to these questions will possibly facilitate the generation of Sap-based anticandidal drugs or immunotherapeutics.
authors.affiliation: Department of Bacteriology and Medical Mycology, Istituto Superiore di Sanità, Rome, Italy.
authors.forename: F
authors.initials: F
authors.lastname: De Bernardis
authors.forename: P A
authors.initials: PA
authors.lastname: Sullivan
authors.forename: A
authors.initials: A
authors.lastname: Cassone
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000235:genetics / Q000378:metabolism*; D002176:Candida albicans / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity*; D002177:Candidiasis / Q000382:microbiology; D004195:Disease Models, Animal; D005260:Female; D006801:Humans; D051381:Rats; D014774:Virulence
chemical_list: D016282:Aspartic Acid Endopeptidases