Infections Caused by Nondiphtheria Corynebacteria

Lipsky, Benjamin A.; Goldberger, Allen C.; Tompkins, Lucy S.; Plorde, James J.

doi:10.1093/clinids/4.6.1220

Cited by 222 publications

(118 citation statements)

References 89 publications

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“…Phospholipase D (PLD) is a potent exotoxin produced by C. pseudotuberculosis and it has been considered as the major virulence factor for this bacterium [51,65].…”

Section: Phospholipase Dmentioning

confidence: 99%

“…This exotoxin is a permeability factor that promotes the hydrolysis of ester bonds in sphingomyelin in mammalian cell membranes, possibly contributing to the spread of the bacteria from the initial site of infection to secondary sites within the host [19,30,65,69,89,106,108]. Moreover, it provokes dermonecrotic lesions, and at higher doses it is lethal to a number of different species of laboratory and domestic animals [34,102].…”

Section: Phospholipase Dmentioning

confidence: 99%

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Corynebacterium pseudotuberculosis: microbiology, biochemical properties, pathogenesis and molecular studies of virulence

et al. 2006

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-Corynebacterium pseudotuberculosis is the etiological agent of caseous lymphadenitis (CLA), a common disease in small ruminant populations throughout the world. Once established, this disease is difficult to eradicate because drug therapy is not effective and because the clinical detection of infected animals is of limited efficiency. We reviewed the microbiological, biochemical and taxonomic features of C. pseudotuberculosis, general aspects of infection, the main virulence determinants and currently available commercial vaccines. We also examined the current molecular strategies for the study of virulence in C. pseudotuberculosis, including the latest research on the identification of novel virulence factors and genes, which will help us to better understand the biology of this microorganism. This knowledge may also contribute to the development of improved CLA vaccines, including subunit and DNA-based types, as well as to improve the diagnosis, treatment and control of this disease.

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“…Phospholipase D (PLD) is a potent exotoxin produced by C. pseudotuberculosis and it has been considered as the major virulence factor for this bacterium [51,65].…”

Section: Phospholipase Dmentioning

confidence: 99%

Section: Phospholipase Dmentioning

confidence: 99%

Corynebacterium pseudotuberculosis: microbiology, biochemical properties, pathogenesis and molecular studies of virulence

et al. 2006

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“…2 E and F). The respiratory pathogen Arcanobacterium haemolyticum also produces SMase D, an extracellular product (19)(20)(21). Significantly, infection with this bacterium is invariably associated with respiratory symptoms (21).…”

Section: Discovery and Identification Of Cftr-inhibiting Activity In mentioning

confidence: 99%

Inhibition of CFTR Cl ⁻ channel function caused by enzymatic hydrolysis of sphingomyelin

Ramu

Lü

2007

Proc. Natl. Acad. Sci. U.S.A.

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Numerous mutations in the cystic fibrosis (CF) transmembrane conductance regulator (CFTR, a Cl − channel) disrupt salt and fluid transport and lead to the formation of thick mucus in patients' airways. Obstruction by mucus predisposes CF patients to chronic infections and inflammation, which become gradually harder to control and eventually fatal. Aggressive antibiotic therapy and supportive measures have dramatically lengthened CF patients' lives. Here, we report that sphingomyelinases (SMase) from human respiratory pathogens strongly inhibit CFTR function. The hydrolysis of sphingomyelin by SMase makes it more difficult to activate CFTR by phosphorylation of its regulatory domain. By inhibiting CFTR currents, SMase-producing respiratory tract bacteria may not only aggravate pulmonary infection in some CF patients but may also elicit a condition, analogous to CFTR deficiency, in non-CF patients suffering from bacterial lung infection.

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“…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).…”

mentioning

confidence: 99%

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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Infections Caused by Nondiphtheria Corynebacteria

Cited by 222 publications

References 89 publications

Corynebacterium pseudotuberculosis: microbiology, biochemical properties, pathogenesis and molecular studies of virulence

Corynebacterium pseudotuberculosis: microbiology, biochemical properties, pathogenesis and molecular studies of virulence

Inhibition of CFTR Cl ⁻ channel function caused by enzymatic hydrolysis of sphingomyelin

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

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Infections Caused by Nondiphtheria Corynebacteria

Cited by 222 publications

References 89 publications

Corynebacterium pseudotuberculosis: microbiology, biochemical properties, pathogenesis and molecular studies of virulence

Corynebacterium pseudotuberculosis: microbiology, biochemical properties, pathogenesis and molecular studies of virulence

Inhibition of CFTR Cl − channel function caused by enzymatic hydrolysis of sphingomyelin

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

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Inhibition of CFTR Cl ⁻ channel function caused by enzymatic hydrolysis of sphingomyelin