title: Localisation of Bgl2p upon antifungal drug treatment in Candida albicans.
abstract: Several proteins are covalently bound to the cell wall glucan (glucan-associated proteins (GAPs)) in Candida albicans and different drugs may cause their modulation. Proteomic analysis is a suitable approach to study differential GAP patterns between control and drug-treated cells. Since antimycotics induce variation in GAP content, we investigated the effect of a sublethal dose of micafungin and observed a clear increase in Bgl2p, an enzyme with glucanosyltransferase activity, with respect to a general decrease in cell wall protein content. Immunoelectron microscopy using mouse antiserum confirmed this increase of Bgl2p on the outer cell wall but also revealed a dramatic increase in the immature Bgl2p isoform in the cytoplasm of drug-treated cells. Since this increased expression of Bgl2p is clearly dependent upon micafungin treatment, this enzyme appears to be one of the survival strategies of C. albicans and thus could be considered the molecular basis of antifungal resistance and also as a potential valuable candidate for future vaccine development.
authors.affiliation: Department of Public Health Sciences G. Sanarelli, University of Rome La Sapienza, Rome, Italy. letizia.angiolella@uniroma1.it
authors.forename: Letizia
authors.initials: L
authors.lastname: Angiolella
authors.forename: Alberto
authors.initials: A
authors.lastname: Vitali
authors.forename: Annarita
authors.initials: A
authors.lastname: Stringaro
authors.forename: Giuseppina
authors.initials: G
authors.lastname: Mignogna
authors.forename: Bruno
authors.initials: B
authors.lastname: Maras
authors.forename: Mariantonietta
authors.initials: M
authors.lastname: Bonito
authors.forename: Marisa
authors.initials: M
authors.lastname: Colone
authors.forename: Anna Teresa
authors.initials: AT
authors.lastname: Palamara
authors.forename: Antonio
authors.initials: A
authors.lastname: Cassone
mesh_terms: D000935:Antifungal Agents / Q000494:pharmacology*; D002176:Candida albicans / Q000737:chemistry / Q000187:drug effects*; D002473:Cell Wall / Q000737:chemistry; D003593:Cytoplasm / Q000737:chemistry; D054714:Echinocandins / Q000494:pharmacology*; D005656:Fungal Proteins / Q000096:biosynthesis*; D005964:Glucosyltransferases / Q000096:biosynthesis*; D055666:Lipopeptides / Q000494:pharmacology*; D000077551:Micafungin; D016253:Microscopy, Immunoelectron; D020543:Proteome / Q000032:analysis / Q000187:drug effects; D015854:Up-Regulation
chemical_list: D000935:Antifungal Agents; D054714:Echinocandins; D005656:Fungal Proteins; D055666:Lipopeptides; D020543:Proteome; D005964:Glucosyltransferases; D000077551:Micafungin