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Antibacterial Properties of Intestinal Phospholipase A2 from the Common Stingray Dasyatis pastinaca |
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| Authors: | Abir Ben Bacha Islem Abid Habib Horchani |
| Institution: | 1. Biochemistry Department, Science College, King Saud University, P.O. Box 22452, Riyadh, 11495, Saudi Arabia 2. Laboratory of Plant Biotechnology Applied to Crop Improvement, Faculty of Science of Sfax, University of Sfax, Sfax, 3038, Tunisia 3. Botany and Microbiology Department, Science College, King Saud University, P.O. Box 22452, Riyadh, 11495, Saudi Arabia 4. LOEX/CUO-recherche, H?pital du Saint-Sacrement, Centre Hospitalier Affilié de Québec, Université Laval, Québec, G1S 4L8, Canada 5. Département d’Ophtalmologie, Faculté de Médecine, Université Laval, Québec, G1S 4L8, Canada |
| Abstract: | Stingray phospholipase A2 group IIA (SPLA2-IIA) was recently isolated and purified to homogeneity from the intestine of the common stingray Dasyatis pastinaca, suggesting that this enzyme plays an important role in systemic bactericidal defense. The present study showed that SPLA2-IIA was highly bactericidal against Gram-positive bacteria with inhibition zones and minimal inhibitory concentration values in the range of 13–25 mm and 2–8 μg/ml, respectively, whereas Gram-negative bacteria exhibited a much higher resistance. The bactericidal efficiency of SPLA2-IIA was shown to be unaffected by high protein and salt concentrations, but dependent upon the presence of calcium ions, and then correlated to the hydrolytic activity of membrane phospholipids. Importantly, we showed that stingray phospholipase A2 group IIA presents no cytotoxicity after its incubation with MDA-MB-231 cells. SPLA2-IIA may be considered as a future therapeutic agent against bacterial infections. |
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