Inactivation of the phospholipase B gene PLB5 in wild-type Candida albicans reduces cell-associated phospholipase A2 activity and attenuates virulence

Stephanie Theiss, Ganchimeg Ishdorj, Audrey Brenot, Marianne Kretschmar, Chung Yu Lan, Thomas Nichterlein, Jörg Hacker, Santosh Nigam, Nina Agabian, Gerwald A. Köhler

Research output: Contribution to journalArticle

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Abstract

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 A2 activity and in vivo organ colonization.

Original languageEnglish
Pages (from-to)405-420
Number of pages16
JournalInternational Journal of Medical Microbiology
Volume296
Issue number6
DOIs
StatePublished - 12 Oct 2006

Fingerprint

Lysophospholipase
Phospholipases
Phospholipases A2
Multigene Family
Candida albicans
Virulence
Fungal Genome
Lysophospholipids
Hydrolases
Membrane Lipids
Substrate Specificity
Genes
Real-Time Polymerase Chain Reaction
Phospholipids
Esters
Proteins
Phenotype
Lipids
Gene Expression
Growth

Keywords

  • Candida
  • GPI anchor
  • Lysophospholipase
  • Phospholipase
  • Selection marker
  • Virulence

Cite this

Theiss, Stephanie ; Ishdorj, Ganchimeg ; Brenot, Audrey ; Kretschmar, Marianne ; Lan, Chung Yu ; Nichterlein, Thomas ; Hacker, Jörg ; Nigam, Santosh ; Agabian, Nina ; Köhler, Gerwald A. / Inactivation of the phospholipase B gene PLB5 in wild-type Candida albicans reduces cell-associated phospholipase A2 activity and attenuates virulence. In: International Journal of Medical Microbiology. 2006 ; Vol. 296, No. 6. pp. 405-420.
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Inactivation of the phospholipase B gene PLB5 in wild-type Candida albicans reduces cell-associated phospholipase A2 activity and attenuates virulence. / Theiss, Stephanie; Ishdorj, Ganchimeg; Brenot, Audrey; Kretschmar, Marianne; Lan, Chung Yu; Nichterlein, Thomas; Hacker, Jörg; Nigam, Santosh; Agabian, Nina; Köhler, Gerwald A.

In: International Journal of Medical Microbiology, Vol. 296, No. 6, 12.10.2006, p. 405-420.

Research output: Contribution to journalArticle

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AU - Theiss, Stephanie

AU - Ishdorj, Ganchimeg

AU - Brenot, Audrey

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AU - Lan, Chung Yu

AU - Nichterlein, Thomas

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AU - Agabian, Nina

AU - Köhler, Gerwald A.

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AB - 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 A2 activity and in vivo organ colonization.

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