Potential Role of Phospholipases in Virulence and Fungal Pathogenesis

Ghannoum, Mahmoud A.

doi:10.1128/cmr.13.1.122-143.2000

Cited by 535 publications

(458 citation statements)

References 202 publications

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“…Ghannoum 4 and D`Eça Júnior et al 7 suggested that the quantity of phospholipase produced by C. albicans varies with each specifi c isolate, and it is correlated with the site of infection.…”

Section: Discussion Financial Support Referencesmentioning

confidence: 99%

“…In general, bloodstream isolates are known to produce much higher levels of phospholipase and proteinase than wound or urine isolates 4,15 .…”

Section: Discussion Financial Support Referencesmentioning

confidence: 99%

“…Several virulence factors of C. albicans have been discovered or proposed, including adhesion factors, hyphal formation, germ tubes (GTs), phenotypic diversity, and the production of extracellular hydrolytic enzymes such as phospholipases and proteinases [2][3][4][5][6] .…”

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confidence: 99%

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Determination of germ tube, phospholipase, and proteinase production by bloodstream isolates of Candida albicans

Mattei

Alves

Severo³

et al. 2013

Rev. Soc. Bras. Med. Trop.

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Introduction: Candida albicans is a commensal and opportunistic agent that causes infection in immunocompromised individuals. Several attributes contribute to the virulence and pathogenicity of this yeast, including the production of germ tubes (GTs) and extracellular hydrolytic enzymes, particularly phospholipase and proteinase. This study aimed to investigate GT production and phospholipase and proteinase activities in bloodstream isolates of C. albicans. Methods: One hundred fi fty-three C. albicans isolates were obtained from blood samples and analyzed for GT, phospholipase, and proteinase production. The assays were performed in duplicate in egg yolk medium containing bovine serum albumin and human serum. Results: Detectable amounts of proteinase were produced by 97% of the isolates, and 78% of the isolates produced phospholipase. GTs were produced by 95% of the isolates. A majority of the isolates exhibited low levels of phospholipase production and high levels of proteinase production. Conclusions: Bloodstream isolates of C. albicans produce virulence factors such as GT and hydrolytic enzymes that enable them to cause infection under favorable conditions.

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Section: Discussion Financial Support Referencesmentioning

confidence: 99%

“…In general, bloodstream isolates are known to produce much higher levels of phospholipase and proteinase than wound or urine isolates 4,15 .…”

Section: Discussion Financial Support Referencesmentioning

confidence: 99%

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Determination of germ tube, phospholipase, and proteinase production by bloodstream isolates of Candida albicans

Mattei

Alves

Severo³

et al. 2013

Rev. Soc. Bras. Med. Trop.

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“…The assay kits are a simple, fluorometric method designed for continuous monitoring of PLA 1 or PLA 2 activity. The substrates are specific for each enzyme and are dye-labelled glycerophosphoethanolamine and glycerophosphocholine with a BO-DIPY(R)FL dye-labelled acyl chain at the sn-1 or the sn-2 position.…”

Section: Pla 1 and Pla 2 Activity Assaymentioning

confidence: 99%

“…Microbial phospholipases further contribute to pathogenesis and virulence through the release or breakdown of bioactive compounds that affect host cell function [1][2][3][4]. Substrates for phospholipases are either phospholipids or lysophospholipids, comprising a polar head group (e.g.…”

Section: Introductionmentioning

confidence: 99%

A novel phospholipase B from Streptomyces sp. NA684 – purification, characterization, gene cloning, extracellular production and prediction of the catalytic residues

et al. 2013

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A novel metal ion-independent phospholipase B (PLB 684 ) from Streptomyces sp. strain NA684 was purified 264-fold from the culture supernatant with 2.85% recovery (6330 UÁmg protein À1 ). The enzyme functions as a monomer with a molecular mass of 38.9 kDa. Maximum activity was found at pH 8.4 and 50°C. The substrate specificity was in the order: phosphatidylcholine ≥ phosphatidic acid ≥ lysophosphatidylcholine > phosphatidylserine > phosphatidylinositol > phosphatidylglycerol. The enzyme did not hydrolyze phosphatidylethanolamine, tristearin and dipalmitin. PLB 684 hydrolyzed lysophosphatidylcholine and diacylphosphatidylcholine, and lysophosphatidylcholine was primarily produced during the early stages of phosphatidylcholine hydrolysis. The apparent K m , V max and k cat for hydrolysis of dimyristoyl phosphatidic acid were 14.5 mM, 15.8 mmolÁmin À1 Ámg protein À1 and 1.02 9 10 4 s À1 , respectively. The positional specificity of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine hydrolysis was investigated using GC. In the reaction equilibrium, the molar ratio of released fatty acids (sn-1 : sn-2) was 45 : 55. The ORF of the gene is 1239 bp in length and codes for a 30-amino acid signal peptide and a 382-amino acid mature enzyme. The deduced amino acid sequence of PLB 684 shows 60% identity to a uncharacterized protein of Streptomyces auratus AGR0001 (UniProt accession number: J1RQY0). The extracellular production of PLB 684 was achieved using a pUC702 expression vector and Streptomyces lividans as the host. Mutagenesis analysis showed that Ser12 is essential for the catalytic function of PLB 684 and that the active site may include residues Ser330 and His332.

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