Identification and characterization of a new enzyme of the group “phospholipase D” isolated from Corynebacterium ovis

Soucek, A; Michalec, C; Soucková, A

doi:10.1016/0005-2744(71)90173-2

Cited by 69 publications

(26 citation statements)

References 23 publications

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“…In conclusion, by building on early but largely overlooked evidence (21), we have demonstrated here that spider and bacterial SMases D have intrinsic lyso-PLD activity toward albumin-bound LPC and thereby generate bioactive LPA. To be consistent with phospholipase terminology, SMaseD should therefore be renamed "SM-and LPC-specific PLD."…”

Section: Resultsmentioning

confidence: 63%

“…Yet, the possibility that degradation of plasma LPC might contribute to SMaseD toxicity has re-ceived little attention to date. On the other hand, the reported K m value for LPC was very high, ϳ8 mM (21), suggesting that LPC is not a physiological substrate; moreover, LPC hydrolysis by partially purified SMaseD preparations could well be due to contaminating lyso-PLD activity.…”

mentioning

confidence: 97%

“…Our interest was stirred by a report of more than 30 years ago, showing that partially purified SMaseD from C. pseudotuberculosis (ovis) can catalyze the release of choline from lysophosphatidylcholine (LPC) but not from phosphatidylcholine (PC) (21). LPC is an abundant plasma component and removal of its choline headgroup yields lysophosphatidic acid (LPA), now known as a pleiotropic lipid mediator acting on specific G protein-coupled receptors in numerous cell types (22,23).…”

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confidence: 99%

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Spider and Bacterial Sphingomyelinases D Target Cellular Lysophosphatidic Acid Receptors by Hydrolyzing Lysophosphatidylcholine

Meeteren

Frederiks

Giepmans

et al. 2004

Journal of Biological Chemistry

122

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Bites byEnvenomation by Loxosceles spiders, endemic to temperate and (sub)tropical regions of the Americas, Africa, and Europe, can lead to local skin injury as well as to serious systemic toxicity, including thrombus formation, vascular leakage, hemolysis, and persistent inflammation (1-3). In severe cases, the hematologic complications can lead to renal failure and death, especially in children (2, 3). Treatment is difficult; antivenoms are not very effective, and the use of corticosteroids or anti-inflammatory medication is controversial (3). The toxin responsible for the local and systemic effects of Loxosceles venom is an unusual sphingomyelinase D (SMaseD) 1 that converts sphingomyelin (SM) in the outer leaflet of the plasma membrane to ceramide 1-phosphate (N-acylsphingosine 1-phosphate) (4 -7). Strikingly, while SMaseD is not found elsewhere in the animal kingdom, a similar enzyme is produced as an exotoxin by some pathogenic bacteria, notably Corynebacterium pseudotuberculosis, Corynebacterium ulcerans, and Arcanobacterium (formerly Corynebacterium) hemolyticum (8 -10). C. pseudotuberculosis causes lymphadenitis in animals but is also pathogenic for humans, while C. ulcerans and A. hemolyticum are pathogens of pharyngitis and other human infections (11); in no case is the molecular basis for virulence known (12). The SMaseD from C. pseudotuberculosis, also named SM-specific phospholipase D (PLD), is an essential virulence determinant that contributes to the persistence and spread of the bacteria within the host (13). The Loxosceles and C. pseudotuberculosis SMases D have the same molecular mass (31-32 kDa) and share about 30% sequence similarity (see "Results"). In model systems, the spider and bacterial enzymes provoke remarkably similar pathophysiological effects, including platelet aggregation, endothelial hyperpermeability, complement-dependent hemolysis, and neutrophil-dependent skin necrosis (4 -7, 9, 14 -16).Despite decades of study it remains unclear how SMaseD can elicit such a wide variety of biological effects, particularly, since ceramide 1-phosphate is not known as a signaling molecule. In contrast to ceramide, which may reorganize lipid microdomains and associated signaling complexes (17, 18), ceramide 1-phosphate is a bilayer-preferring phospholipid that is unlikely to significantly perturb membrane structure. Furthermore, mammalian cells treated with SMaseD from either Loxosceles deserta or C. pseudotuberculosis do not convert newly formed ceramide 1-phosphate to ceramide nor does SMaseD treatment affect membrane permeability or cell viability (19,20).Given the lack of understanding of SMaseD bioactivity, we set out to re-examine the substrate specificity and cellular effects of the enzyme. Our interest was stirred by a report of more than 30 years ago, showing that partially purified SMaseD from C. pseudotuberculosis (ovis) can catalyze the release of choline from lysophosphatidylcholine (LPC) but not from phosphatidylcholine (PC) (21). LPC is an abundant plasma component and removal ...

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Section: Resultsmentioning

confidence: 63%

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confidence: 97%

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confidence: 99%

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Spider and Bacterial Sphingomyelinases D Target Cellular Lysophosphatidic Acid Receptors by Hydrolyzing Lysophosphatidylcholine

Meeteren

Frederiks

Giepmans

et al. 2004

Journal of Biological Chemistry

122

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“…SMase D cleaves the choline moiety from sphingomyelin ( Fig. 1 A) (Souček et al, 1971), a phospholipid found predominantly in the plasma membrane's outer leaflet, leaving behind ceramide-1-phosphate (C1P). C. pseudotuberculosis is perhaps the most studied model of SMase D in bacterial virulence.…”

Section: Introductionmentioning

confidence: 99%

Sphingomyelinase D inhibits store-operated Ca²⁺entry in T lymphocytes by suppressing ORAI current

Combs¹,

Lü²

2015

J Cell Biol

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“…First, no detailed knowledge of the characteristics of the exotoxin of C. ovis (which it was thought by Petrie & McClean to resemble), became available until the papers of Soucek & Souckova (1971, Carne & Onon (1978) and Onon (1979). These have shown that C. ovis toxin is a basic glycoprotein, MW 14500+1000, which is a phospholipase D; it attacks sphingomyelin to produce ceramide phosphate and choline; when inoculated intradermally or subcutaneously in guinea-pigs, rabbits or sheep it causes marked leakage of plasma from blood and lymph vessels, producing local oedema; it does not produce congestion of the adrenal cortex of the guinea-pig, which is characteristic of diphtheria toxin.…”

Section: Introductionmentioning

confidence: 99%

The exotoxins ofCorynebacterium ulcerans

Carne

Onon

1982

J. Hyg.

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SUMMARYThe exotoxins produced by ten strains of C. ulcerans (two human, six bovine and two equine) have been studied. On the criteria oftoxin-antitoxin neutralisation and immunoprecipitation tests using highly specific diphtheria and C. ovis antitoxins with crude toxic filtrates, (NH4)2SO4 concentrates, and partially purified chromatographic preparations of these, together with the presence or absence of inhibition of the action of staphylococcal beta-haemolysin, and the reaction produced when injected intradermally into rabbits, two toxins could be identified, namely diphtheria toxin and C. ovis toxin. There was no evidence for the production of a third toxin specific for C. ulcerans. Five strains produced both diphtheria and C. ovis toxins. In four diphtheria toxin predominated, but in the fifth C. ovis toxin predominated. Two strains produced only diphtheria toxin and two only C. ovis toxin, though there was good but not complete evidence that a third strain (Revell) also fell into this latter group. Considerable variation occurred in the concentration of each toxin and, where both were present, in the proportion of each.

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Identification and characterization of a new enzyme of the group “phospholipase D” isolated from Corynebacterium ovis

Cited by 69 publications

References 23 publications

Spider and Bacterial Sphingomyelinases D Target Cellular Lysophosphatidic Acid Receptors by Hydrolyzing Lysophosphatidylcholine

Spider and Bacterial Sphingomyelinases D Target Cellular Lysophosphatidic Acid Receptors by Hydrolyzing Lysophosphatidylcholine

Sphingomyelinase D inhibits store-operated Ca²⁺entry in T lymphocytes by suppressing ORAI current

The exotoxins ofCorynebacterium ulcerans

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Identification and characterization of a new enzyme of the group “phospholipase D” isolated from Corynebacterium ovis

Cited by 69 publications

References 23 publications

Spider and Bacterial Sphingomyelinases D Target Cellular Lysophosphatidic Acid Receptors by Hydrolyzing Lysophosphatidylcholine

Spider and Bacterial Sphingomyelinases D Target Cellular Lysophosphatidic Acid Receptors by Hydrolyzing Lysophosphatidylcholine

Sphingomyelinase D inhibits store-operated Ca2+entry in T lymphocytes by suppressing ORAI current

The exotoxins ofCorynebacterium ulcerans

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Sphingomyelinase D inhibits store-operated Ca²⁺entry in T lymphocytes by suppressing ORAI current