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• W23636710 abstract "Candida albicans is usually present as a harmless commensal of the mucosal surfaces of the alimentary canal and urogenital tracts, but it is a major cause of hospitalacquired infection in immunocompromised individuals. Candida spp. are the fourth most common cause of bloodstream infection. Moreover, the mortality rate of systemic candidiasis is very high due to the difficulty in diagnosis and treatment. Candida albicans is a polymorphic fungus that can change its morphology ranging from hyphae to yeast. The ability to switch between these morphologies is believed to be involved in the pathogenesis and virulence of this organism. The Candida albicans PHR1 (pH-regulated) gene is an alkali-expressed gene that encodes a 548 amino acid residue GPI-anchored cell surface glycoprotein. The deletion of PHR1 in C. albicans resulted in pH-conditional defects of cell morphology and virulence. The enzyme encoded by PHR1 is required for proper cross-linking of -1,3-glucans and -1,6-glucans in the cell wall. Both this enzyme and the cell wall itself are absent in host cells, which makes it an interesting target for new antifungal drug development. We developed methods to study protein-protein interactions which combined protein cross-linking, Triton ® X-114 extraction, ion exchange chromatography, 2 dimensional SDS-PAGE and mass spectrometry of an epitope tagged Phr1p that proved iv successful in analyzing interactions of membrane bound Phr1p. Therefore, these procedures might be useful for studying other membrane proteins. The results showed that the Phr1p forms a complex about double the size of Phr1p and mass spectrometry indicated that Phr1p was the only major component of this complex. Together this suggests that Phr1p forms a dimer. The dimer was enriched in the detergent-rich phase after Triton ® X-114 extraction and phase separation, an observation consistent with the dimer retaining a hydrophobic GPI-anchor moiety. Western blotting results showed about 25-60% of Phr1p was in a dimeric form, which may indicate that the function of the dimeric form of Phr1p is distinct from that of the monomeric form." @default.
• W23636710 created "2016-06-24" @default.
• W23636710 creator A5003420241 @default.
• W23636710 date "2011-01-01" @default.
• W23636710 modified "2023-09-23" @default.
• W23636710 title "Function of PHR1 in Candida albicans cell wall assembly" @default.
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• W23636710 hasPublicationYear "2011" @default.
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