Toxoplasma gondii secretes a calcium-independent phospholipase A(2)
Phospholipases A(2) (PLA(2)) play an important role in Toxoplasma gondii host cell penetration. They are also key enzymes in the host cell response to the parasite invasion. PLA(2) hydrolyse cellular phospholipids, releasing multiple inflammatory lipidic mediators. We have investigated the biochemic...
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| Veröffentlicht in: | International journal for parasitology 2000-10, Vol.30 (11), p.1137-1142 |
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| container_title | International journal for parasitology |
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| creator | Cassaing, S Fauvel, J Bessières, M H Guy, S Séguéla, J P Chap, H |
| description | Phospholipases A(2) (PLA(2)) play an important role in Toxoplasma gondii host cell penetration. They are also key enzymes in the host cell response to the parasite invasion. PLA(2) hydrolyse cellular phospholipids, releasing multiple inflammatory lipidic mediators. We have investigated the biochemical characterisation of T. gondii PLA(2) activity in a mouse-cultured tachyzoite homogenate and in the peritoneal exudate from infected mice, using the hydrolysis of a fluorescent phosphatidylglycerol labelled at the sn-2 position. Spectrofluorimetry and thin-layer chromatography showed a PLA(2) activity (about 0.5-2 nmol/min per mg), calcium-independent, secreted into infected mice peritoneal exudate, with a broad pH activity ranging between 6.5 and 9.5 and resistant to a great number of potential PLA(2) inhibitors except dithio-nitrobenzoic acid (1 mM). An associated phospholipase A(1) activity was also displayed. These results suggest that Toxoplasma gondii displays specific phospholipases different from host enzymes and probably involved at critical steps of infectious cycle. |
| doi_str_mv | 10.1016/S0020-7519(00)00101-6 |
| format | Article |
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They are also key enzymes in the host cell response to the parasite invasion. PLA(2) hydrolyse cellular phospholipids, releasing multiple inflammatory lipidic mediators. We have investigated the biochemical characterisation of T. gondii PLA(2) activity in a mouse-cultured tachyzoite homogenate and in the peritoneal exudate from infected mice, using the hydrolysis of a fluorescent phosphatidylglycerol labelled at the sn-2 position. Spectrofluorimetry and thin-layer chromatography showed a PLA(2) activity (about 0.5-2 nmol/min per mg), calcium-independent, secreted into infected mice peritoneal exudate, with a broad pH activity ranging between 6.5 and 9.5 and resistant to a great number of potential PLA(2) inhibitors except dithio-nitrobenzoic acid (1 mM). An associated phospholipase A(1) activity was also displayed. These results suggest that Toxoplasma gondii displays specific phospholipases different from host enzymes and probably involved at critical steps of infectious cycle.</abstract><cop>England</cop><pmid>11027777</pmid><doi>10.1016/S0020-7519(00)00101-6</doi><tpages>6</tpages></addata></record> |
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| subjects | Animals Calcium Chloride - chemistry Chromatography, Thin Layer Deoxyribonuclease BamHI - chemistry DNA Primers - chemistry DNA, Protozoan - chemistry DNA, Protozoan - isolation & purification Electrophoresis, Agar Gel Female Fluorometry Hydrogen-Ion Concentration Macrophages, Peritoneal - chemistry Macrophages, Peritoneal - parasitology Mice Mice, Inbred BALB C Mice, Inbred C57BL Phospholipases A - analysis Phospholipases A - antagonists & inhibitors Phospholipases A - chemistry Polymerase Chain Reaction Toxoplasma - enzymology Toxoplasmosis, Animal - enzymology Toxoplasmosis, Animal - parasitology |
| title | Toxoplasma gondii secretes a calcium-independent phospholipase A(2) |
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