Journal
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY
Volume 296, Issue 6, Pages 405-420Publisher
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.ijmm.2006.03.003
Keywords
GPI anchor; phospholipase; lysophospholipase; Candida; selection marker; virulence
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Funding
- NIAID NIH HHS [R01 AI33317] Funding Source: Medline
- NIDCR NIH HHS [P01 DE016839-01, R21 DE014705, R21 DE014705-01A1, R21 DE014705-02, P01 DE016839] Funding Source: Medline
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Phospholipases are critical for modification and redistribution of lipid substrates, membrane remodeling and microbial virulence. Among the many different classes of phospholipases, fungal phospholipase B (Plb) proteins show the broadest range of substrate specificity and hydrolytic activity, hydrolyzing acyl ester bonds in phospholipids and lysophospholipids and further catalyzing lysophospholipase-transacylase reactions. The genome of the opportunistic fungal pathogen Candida albicans encodes a PLB multigene family with five putative members; we present the first characterization of this group of potential virulence determinants. CaPLB5, the third member of this multigene family characterized herein is a putative secretory protein with a predicted GPI-anchor attachment site. Real-time RT-PCR gene expression analysis of CaPLB5 and the additional CaPLB gene family members revealed that filamentous growth and physiologically relevant environmental conditions are associated with increased PLB gene activity. The phenotypes expressed by null mutant and revertant strains of CaPLB5 indicate that this lipid hydrolase plays an important role for cell-associated phospholipase A(2) activity and in vivo organ colonization. (c) 2006 Elsevier GmbH. All rights reserved.
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