title: Candida albicans proteinases and host/pathogen interactions.
abstract: Candida infections are common, debilitating and often recurring fungal diseases and a problem of significant clinical importance. Candida albicans, the most virulent of the Candida spp., can cause severe mucosal and life-threatening systemic infections in immunocompromised hosts. Attributes that contribute to C. albicans virulence include adhesion, hyphal formation, phenotypic switching and extracellular hydrolytic enzyme production. The extracellular hydrolytic enzymes, especially the secreted aspartyl proteinases (Saps), are one of few gene products that have been shown to directly contribute to C. albicans pathogenicity. Because C. albicans is able to colonize and infect almost every tissue in the human host, it may be crucial for the fungus to possess a number of similar but independently regulated and functionally distinct secreted proteinases to provide sufficient flexibility in order to survive and promote infection at different niche sites. The aim of this review is to explore the functional roles of the C. albicans proteinases and how they may contribute to the host/pathogen interaction in vivo.
authors.affiliation: Department of Oral Medicine, Pathology & Immunology, GKT Dental Institute, Kings College London (Guy's Campus), London, UK.
authors.forename: Julian
authors.initials: J
authors.lastname: Naglik
authors.forename: Antje
authors.initials: A
authors.lastname: Albrecht
authors.forename: Oliver
authors.initials: O
authors.lastname: Bader
authors.forename: Bernhard
authors.initials: B
authors.lastname: Hube
mesh_terms: D002176:Candida albicans / Q000201:enzymology* / Q000502:physiology*; D002177:Candidiasis; D005656:Fungal Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D015971:Gene Expression Regulation, Enzymologic; D015966:Gene Expression Regulation, Fungal; D006790:Host-Parasite Interactions; D006801:Humans; D005810:Multigene Family; D012697:Serine Endopeptidases / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: D005656:Fungal Proteins; D012697:Serine Endopeptidases