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In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake Bothrops asper.
- Source :
-
Toxins [Toxins (Basel)] 2012 Dec 14; Vol. 4 (12), pp. 1500-16. Date of Electronic Publication: 2012 Dec 14. - Publication Year :
- 2012
-
Abstract
- The antimicrobial and antiparasite activity of phospholipase A(2) (PLA(2)) from snakes and bees has been extensively explored. We studied the antiplasmodial effect of the whole venom of the snake Bothrops asper and of two fractions purified by ion-exchange chromatography: one containing catalytically-active phospholipases A(2) (PLA(2)) (fraction V) and another containing a PLA(2) homologue devoid of enzymatic activity (fraction VI). The antiplasmodial effect was assessed on in vitro cultures of Plasmodium falciparum. The whole venom of B. asper, as well as its fractions V and VI, were active against the parasite at 0.13 ± 0.01 µg/mL, 1.42 ± 0.56 µg/mL and 22.89 ± 1.22 µg/mL, respectively. Differences in the cytotoxic activity on peripheral blood mononuclear cells between the whole venom and fractions V and VI were observed, fraction V showing higher toxicity than total venom and fraction VI. Regarding toxicity in mice, the whole venom showed the highest lethal effect in comparison to fractions V and VI. These results suggest that B. asper PLA(2) and its homologue have antiplasmodial potential.
- Subjects :
- Amino Acid Sequence
Animals
Antiprotozoal Agents chemistry
Cell Survival drug effects
Cells, Cultured
Crotalid Venoms chemistry
Erythrocytes drug effects
Humans
Lethal Dose 50
Leukocytes, Mononuclear drug effects
Mice
Molecular Sequence Data
Phospholipases chemistry
Plasmodium falciparum growth & development
Sequence Alignment
Antiprotozoal Agents pharmacology
Bothrops
Crotalid Venoms pharmacology
Phospholipases pharmacology
Plasmodium falciparum drug effects
Subjects
Details
- Language :
- English
- ISSN :
- 2072-6651
- Volume :
- 4
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Toxins
- Publication Type :
- Academic Journal
- Accession number :
- 23242318
- Full Text :
- https://doi.org/10.3390/toxins4121500