[47] Phosphatidylinositol-specific phospholipases C from Bacillus cereus and Bacillus thuringiensis

Griffith, O. Hayes; Volwerk, Johannes J.; Kuppe, A

doi:10.1016/0076-6879(91)97175-x

Cited by 67 publications

(54 citation statements)

References 14 publications

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“…PI-PLC activity of Lactobacillus rhamnosus markedly depends on the amount of carbohydrate in the culture medium (48). Similar reports showed that PI-PLC-producing bacteria, including B. cereus, Bacillus thuringiensis, L. monocytogenes, and Staphylococcus aureus, required glucose-free medium for PLC activity to be detected (49)(50)(51). We demonstrated the absence of growth of M. abscessus in low-nutrient medium like PAS (data not shown) and correlatively a growth in the presence of amoebae, indicating that amoebae helped M. abscessus survive in a low-nutrient and/or eukaryotic environment.…”

Section: Discussionsupporting

confidence: 48%

Mycobacterium abscessus Phospholipase C Expression Is Induced during Coculture within Amoebae and Enhances M. abscessus Virulence in Mice

et al. 2015

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Mycobacterium abscessus is a pathogenic, rapidly growing mycobacterium involved in pulmonary and cutaneo-mucous infections worldwide, to which cystic fibrosis patients are exquisitely susceptible. The analysis of the genome sequence of M. abscessus showed that this bacterium is endowed with the metabolic pathways typically found in environmental microorganisms that come into contact with soil, plants, and aquatic environments, where free-living amoebae are frequently present. M. abscessus also contains several genes that are characteristically found only in pathogenic bacteria. One of them is MAB_0555, encoding a putative phospholipase C (PLC) that is absent from most other rapidly growing mycobacteria, including Mycobacterium chelonae and Mycobacterium smegmatis. Here, we report that purified recombinant M. abscessus PLC is highly cytotoxic to mouse macrophages, presumably due to hydrolysis of membrane phospholipids. We further showed by constructing and using an M. abscessus PLC knockout mutant that loss of PLC activity is deleterious to M. abscessus intracellular survival in amoebae. The importance of PLC is further supported by the fact that M. abscessus PLC was found to be expressed only in amoebae. Aerosol challenge of mice with M. abscessus strains that were precultured in amoebae enhanced M. abscessus lung infectivity relative to M. abscessus grown in broth culture. Our study underlines the importance of PLC for the virulence of M. abscessus. Despite the difficulties of isolating M. abscessus from environmental sources, our findings suggest that M. abscessus has evolved in close contact with environmental protozoa, which supports the argument that amoebae may contribute to the virulence of opportunistic mycobacteria.T he recognition of the role of Mycobacterium abscessus in human pathology has taken several decades, due to confusion in many studies between this mycobacterium and the very closely related species Mycobacterium chelonae. It was only in 1992 that these two species were distinguished and M. abscessus elevated to the rank of species (1).These two phylogenetically closely related, rapidly growing mycobacteria (RGM), which have identical 16S ribosomal rRNA gene sequences, are distinguished by different pathogenicity patterns. M. chelonae, generally less pathogenic than M. abscessus, is implicated in skin and soft tissue infections and only occasionally involved in lung infections. M. abscessus is currently the most frequently isolated RGM in human pathology and the main RGM involved in lung infections (2, 3), with a particular link to cystic fibrosis (CF) patients (4-6). M. abscessus is also the main RGM responsible for iatrogenic infections in humans (postinjection abscesses, cardiac surgery infections, and plastic surgery infections) (7-9).The environmental source of M. abscessus that might serve as a reservoir for human infection is currently unknown (10). Although the gene pool of M. abscessus (11) suggests that this bacterium has evolved in an aquatic environment at the interface with plant...

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Section: Discussionsupporting

confidence: 48%

Mycobacterium abscessus Phospholipase C Expression Is Induced during Coculture within Amoebae and Enhances M. abscessus Virulence in Mice

et al. 2015

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“…1B shows that EDTA caused a 40% inhibition of AGP release into the supernatant of rose plasma membrane vesicles. Millimolar ZnCl 2 inhibits both bacterial (24,26) and peanut (25) PI-PLCs. Relatively little AGP was detected in the supernatant of rose plasma membrane vesicles in the presence of ZnCl 2 (Fig.…”

Section: Resultsmentioning

confidence: 99%

Presence of a Glycosylphosphatidylinositol Lipid Anchor on Rose Arabinogalactan Proteins

Svetek¹,

Yadav

Nothnagel

1999

Journal of Biological Chemistry

135

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Arabinogalactan proteins constitute a class of plant cell surface proteoglycans with widespread occurrence and suggested functions in various aspects of plant growth and development, including cell proliferation, expansion, marking, and death. Previous investigations of subcellular fractions from suspension-cultured cells of "Paul's Scarlet" rose (Rosa sp.) have revealed extensive structural similarity between some soluble arabinogalactan proteins from the cell wall space and some plasma membrane-associated arabinogalactan proteins, thus inspiring the present investigation of the mechanism through which these inherently water-soluble molecules are held on the plasma membrane. Several lines of evidence gained through a combination of methods including reversed-phase chromatography, treatment with phosphatidylinositol-specific phospholipase C, and chemical structural analysis now show that some rose arabinogalactan proteins carry a ceramide class glycosylphosphatidylinositol lipid anchor. The predominant form of the ceramide is composed of tetracosanoic acid and 4-hydroxysphinganine. Plasma membrane vesicles readily shed arabinogalactan proteins by an inherent mechanism that appears to involve a phospholipase. This finding has significance toward understanding the biosynthesis, localization, and function of arabinogalactan proteins and toward stimulating other studies that may expand the currently very short list of higher plant proteins found to carry such membrane lipid anchors.

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“…If a hydroxyl group is positioned appropriately in the substrate it can also compete for the phosphoryl enzyme yielding a cyclic product. Cyclic products of phospholipase action have been detected in the action of phosphatidylinositol-specific phospholipase C (PLase C) on phosphatidylinositol yielding 1,2-cyclic inositol phosphate as the initial product (7,8), and in the PLase C hydrolysis of phosphatidylglycerol to 1,3-cyclic glycerophosphate (9). Similar cyclization takes place in the hydrolysis of glycerophosphorylcholine or glycerophosphorylethanolamine by glycerophosphinicocholine diesterase, where 1,2-cyclic glycerophosphate is formed (10,11).…”

mentioning

confidence: 99%

Conversion of Lysophospholipids to Cyclic Lysophosphatidic Acid by Phospholipase D

Friedman

Haimovitz

Markman

et al. 1996

Journal of Biological Chemistry

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Phospholipase D from Streptomyces chromofuscus hydrolyzes lysophosphatidylcholine or lysophosphatidylethanolamine in aqueous 1% Triton X-100 solution. In situ monitoring of this reaction by 31 P NMR revealed the formation of cyclic lysophosphatidic acid (1-acyl 2,3-cyclic glycerophosphate) as an intermediate which was hydrolyzed further by the enzyme at a functionally distinct active site to lysophosphatidic acid (lyso-PA). Synthetic cyclic lyso-PA (1-octanoyl 2,3-cyclic glycerophosphate) was found to be stable in aqueous neutral solutions at room temperature. It was hydrolyzed by the bacterial phospholipase D to lyso-PA at a rate which was approximately 4-fold slower than the rate of formation of cyclic lyso-PA. The addition of 5-10 mM sodium vanadate could partially inhibit the ring opening reaction and thus increase substantially the cyclic lyso-PA accumulation. Cyclic lyso-PA may act as a dormant configuration of the physiologically active lyso-PA or may even possess specific activities which await verification. The first step in the lytic activity of phospholipase D is the formation of a phosphoryl enzyme intermediate which is analogous to the acyl enzyme in the action of common esterases (3,4). This intermediate is generally cleaved by the ambient water molecules with the net hydrolysis of one phosphoester bond. However, alcoholic hydroxyl residues can compete for the cleavage of the phosphoryl enzyme intermediate to yield a phosphodiester product (5, 6). If a hydroxyl group is positioned appropriately in the substrate it can also compete for the phosphoryl enzyme yielding a cyclic product. Cyclic products of phospholipase action have been detected in the action of phosphatidylinositol-specific phospholipase C (PLase C) on phosphatidylinositol yielding 1,2-cyclic inositol phosphate as the initial product (7,8), and in the PLase C hydrolysis of phosphatidylglycerol to 1,3-cyclic glycerophosphate (9). Similar cyclization takes place in the hydrolysis of glycerophosphorylcholine or glycerophosphorylethanolamine by glycerophosphinicocholine diesterase, where 1,2-cyclic glycerophosphate is formed (10, 11). All of these cyclic phosphates are relatively stable at neutral pH but can be hydrolyzed by specific phosphodiesterases to form the respective phosphate monoesters (12, 13). It seems, therefore, that when the phosphoryl residue attached to the enzyme includes a free hydroxyl group, the formation of a cyclic phosphodiester by intramolecular transphosphorylation can take place. In analogy to the above reactions with a hydroxyl group, it has been suggested (9) that phospholipids with a free primary amine group (i.e. phosphatidylethanolamine and phosphatidylserine) may yield a cyclic phosphoramidate intermediate upon the action of PLase C. These putative five-membered cyclic phosphoramidates are expected to be hydrolyzed spontaneously (9).The action of PLase D on phospholipids forms a phosphatidyl enzyme intermediate which can either react with water to yield phosphatidic acid (PA) or with an alcohol (5, 6) to yi...

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[47] Phosphatidylinositol-specific phospholipases C from Bacillus cereus and Bacillus thuringiensis

Cited by 67 publications

References 14 publications

Mycobacterium abscessus Phospholipase C Expression Is Induced during Coculture within Amoebae and Enhances M. abscessus Virulence in Mice

Mycobacterium abscessus Phospholipase C Expression Is Induced during Coculture within Amoebae and Enhances M. abscessus Virulence in Mice

Presence of a Glycosylphosphatidylinositol Lipid Anchor on Rose Arabinogalactan Proteins

Conversion of Lysophospholipids to Cyclic Lysophosphatidic Acid by Phospholipase D

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