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

doi:10.1016/j.ijmm.2006.03.003

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 journal › Article › peer-review

77 Scopus citations

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 language	English
Pages (from-to)	405-420
Number of pages	16
Journal	International Journal of Medical Microbiology
Volume	296
Issue number	6
DOIs	https://doi.org/10.1016/j.ijmm.2006.03.003
State	Published - 12 Oct 2006

Keywords

Candida
GPI anchor
Lysophospholipase
Phospholipase
Selection marker
Virulence

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10.1016/j.ijmm.2006.03.003

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Theiss, S., Ishdorj, G., Brenot, A., Kretschmar, M., Lan, C. Y., Nichterlein, T., Hacker, J., Nigam, S., Agabian, N., & Köhler, G. A. (2006). Inactivation of the phospholipase B gene PLB5 in wild-type Candida albicans reduces cell-associated phospholipase A₂ activity and attenuates virulence. International Journal of Medical Microbiology, 296(6), 405-420. https://doi.org/10.1016/j.ijmm.2006.03.003

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

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.",

keywords = "Candida, GPI anchor, Lysophospholipase, Phospholipase, Selection marker, Virulence",

author = "Stephanie Theiss and Ganchimeg Ishdorj and Audrey Brenot and Marianne Kretschmar and Lan, {Chung Yu} and Thomas Nichterlein and J{\"o}rg Hacker and Santosh Nigam and Nina Agabian and K{\"o}hler, {Gerwald A.}",

note = "Funding Information: This study was supported by the Bundesministerium f{\"u}r Bildung und Forschung (BMBF Grant O1 K18906-0), by the Deutsche Forschungsgemeinschaft (Grant Kr 2002/1-1) and partially by Grant R21 DE014705 to G.A. K{\"o}hler. Furthermore, G.A. K{\"o}hler was recipient of a grant from the “Stipendienprogramm Infektionsforschung” of the BMBF. N. Agabian was supported by NIH grants R01 AI33317 and P01 DE016839-01. We thank William Fonzi for strain CAI4, Remo Morelli for strain SS, and Joachim Morschh{\"a}user for pSFI1. We are also thankful to Stew Scherer for the fosmid library. Genome sequence data for Candida albicans SC5314 was generated at the Stanford DNA Sequencing and Technology Center with the support of the NIDCR, the NIH and the Burroughs Wellcome Fund.",

year = "2006",

month = oct,

day = "12",

doi = "10.1016/j.ijmm.2006.03.003",

language = "English",

volume = "296",

pages = "405--420",

journal = "International Journal of Medical Microbiology",

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Theiss, S, Ishdorj, G, Brenot, A, Kretschmar, M, Lan, CY, Nichterlein, T, Hacker, J, Nigam, S, Agabian, N & Köhler, GA 2006, 'Inactivation of the phospholipase B gene PLB5 in wild-type Candida albicans reduces cell-associated phospholipase A₂ activity and attenuates virulence', International Journal of Medical Microbiology, vol. 296, no. 6, pp. 405-420. https://doi.org/10.1016/j.ijmm.2006.03.003

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

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Inactivation of the phospholipase B gene PLB5 in wild-type Candida albicans reduces cell-associated phospholipase A2 activity and attenuates virulence

AU - Theiss, Stephanie

AU - Ishdorj, Ganchimeg

AU - Brenot, Audrey

AU - Kretschmar, Marianne

AU - Lan, Chung Yu

AU - Nichterlein, Thomas

AU - Hacker, Jörg

AU - Nigam, Santosh

AU - Agabian, Nina

AU - Köhler, Gerwald A.

N1 - Funding Information: This study was supported by the Bundesministerium für Bildung und Forschung (BMBF Grant O1 K18906-0), by the Deutsche Forschungsgemeinschaft (Grant Kr 2002/1-1) and partially by Grant R21 DE014705 to G.A. Köhler. Furthermore, G.A. Köhler was recipient of a grant from the “Stipendienprogramm Infektionsforschung” of the BMBF. N. Agabian was supported by NIH grants R01 AI33317 and P01 DE016839-01. We thank William Fonzi for strain CAI4, Remo Morelli for strain SS, and Joachim Morschhäuser for pSFI1. We are also thankful to Stew Scherer for the fosmid library. Genome sequence data for Candida albicans SC5314 was generated at the Stanford DNA Sequencing and Technology Center with the support of the NIDCR, the NIH and the Burroughs Wellcome Fund.

PY - 2006/10/12

Y1 - 2006/10/12

N2 - 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.

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.

KW - Candida

KW - GPI anchor

KW - Lysophospholipase

KW - Phospholipase

KW - Selection marker

KW - Virulence

UR - http://www.scopus.com/inward/record.url?scp=33748460170&partnerID=8YFLogxK

U2 - 10.1016/j.ijmm.2006.03.003

DO - 10.1016/j.ijmm.2006.03.003

M3 - Article

C2 - 16759910

AN - SCOPUS:33748460170

SN - 1438-4221

VL - 296

SP - 405

EP - 420

JO - International Journal of Medical Microbiology

JF - International Journal of Medical Microbiology

IS - 6

ER -

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

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