PGA4, a GAS homologue from Candida albicans, is up-regulated early in infection processes

Eckert, S.E. and Heinz, W. and Zakikhany, K. and Thewes, S. and Haynes, K. and Hube, B. and Muhlschlegel, F.A. (2007) PGA4, a GAS homologue from Candida albicans, is up-regulated early in infection processes. Fungal Genetics and Biology, 44 (5). pp. 368-377. ISSN 1087-1845 . (The full text of this publication is not available from this repository)

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Abstract

Transglucosidases play a significant role in fungal cell wall biosynthesis. We identified three as yet undescribed genes encoding beta-glucan transglucosidases, homologues of the pH-regulated PHR1 and PHR2, in the genome of the pathogenic yeast Candida albicans. Transcript levels of the gene PGA4 encoding a putative GPI-anchored protein were elevated in C. albicians wild-type cells during infection of reconstituted human epithelial and mouse liver tissue, and transiently increased after induction of hyphal formation with serum. The serum-specific increase in PGA4 transcript was found to be dependent on the transcription factors Ras1p, Cyr1p, and Tec1p. The remaining C. albicans Phr homologues, PHR3 and PGA5, showed low expression levels. Unlike PHR1 and PHR2, the expression of PHR3, PGA4, and PGA5 was not dependent on the pH of the growth medium. Neither PHR3 deletion nor PGA4 disruption resulted in a distinct growth or morphology phenotype. A PGA4 disruption strain was found to have wild-type capacity of infecting reconstituted oral epithelial tissue. Our data suggest that PGA4, and potentially PHR3 and PGA5, are expressed under distinct conditions, which differ from those of PHR1 and PHR2.

Item Type: Article
Uncontrolled keywords: Candida albicans; Phr/Pga/Gas proteins; cell wall; glucan transferases; transglucosidases; expression; infection
Subjects: Q Science > QH Natural history > QH426 Genetics
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Louise Dorman
Date Deposited: 31 Mar 2008 17:41
Last Modified: 14 Jan 2010 14:07
Resource URI: http://kar.kent.ac.uk/id/eprint/2522 (The current URI for this page, for reference purposes)
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