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Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: biochemical and toxicological characterization.
- Source :
-
Biochimie [Biochimie] 2010 Mar; Vol. 92 (3), pp. 273-83. Date of Electronic Publication: 2009 Dec 22. - Publication Year :
- 2010
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Abstract
- Phospholipases A(2) (PLA(2)) are major components of snake venoms, exerting a variety of relevant toxic actions such as neurotoxicity and myotoxicity, among others. Since the majority of toxic PLA(2)s are basic proteins, acidic isoforms and their possible roles in venoms are less understood. In this study, an acidic enzyme (BaspPLA(2)-II) was isolated from the venom of Bothrops asper (Pacific region of Costa Rica) and characterized. BaspPLA(2)-II is monomeric, with a mass of 14,212 +/- 6 Da and a pI of 4.9. Its complete sequence of 124 amino acids was deduced through cDNA and protein sequencing, showing that it belongs to the Asp49 group of catalytically active enzymes. In vivo and in vitro assays demonstrated that BaspPLA(2)-II, in contrast to the basic Asp49 counterparts present in the same venom, lacks myotoxic, cytotoxic, and anticoagulant activities. BaspPLA(2)-II also differed from other acidic PLA(2)s described in Bothrops spp. venoms, as it did not show hypotensive and anti-platelet aggregation activities. Furthermore, this enzyme was not lethal to mice at intravenous doses up to 100 microg (5.9 microg/g), indicating its lack of neurotoxic activity. The only toxic effect recorded in vivo was a moderate induction of local edema. Therefore, the toxicological characteristics of BaspPLA(2)-II suggest that it does not play a key role in the pathophysiology of envenomings by B. asper, and that its purpose might be restricted to digestive functions. Immunochemical analyses using antibodies raised against BaspPLA(2)-II revealed that acidic and basic PLA(2)s form two different antigenic groups in B. asper venom.<br /> (Copyright (c) 2009 Elsevier Masson SAS. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Cells, Cultured
Costa Rica
Edema chemically induced
Humans
Isoenzymes chemistry
Isoenzymes genetics
Mice
Models, Molecular
Molecular Sequence Data
Muscle, Skeletal cytology
Muscle, Skeletal drug effects
Muscle, Skeletal pathology
Phospholipases A2 chemistry
Phospholipases A2 genetics
Phylogeny
Protein Structure, Tertiary
Rabbits
Sequence Alignment
Bothrops
Crotalid Venoms enzymology
Isoenzymes metabolism
Isoenzymes toxicity
Phospholipases A2 metabolism
Phospholipases A2 toxicity
Subjects
Details
- Language :
- English
- ISSN :
- 1638-6183
- Volume :
- 92
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochimie
- Publication Type :
- Academic Journal
- Accession number :
- 20026168
- Full Text :
- https://doi.org/10.1016/j.biochi.2009.12.006