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ISOLATION AND EXPRESSION OF A HYPOTENSIVE AND ANTI-PLATELET ACIDIC PHOSPHOLIPASE A2 FROM BOTHROPS MOOJENI SNAKE VENOM
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Abstract
Phospholipases A2 are important components of snake venoms, the basic isoforms have been more extensively
studied than the acidic groups, maybe due to their higher toxicity. Trying to better understand the
role of the acidic isoforms on the envenomation process, an acidic phospholipase A2 was purified from
Bothrops moojeni snake venom through two chromatographic steps (BmooPLA2). The enzyme showed a
relative molecular mass of 13,601 Da, pI 5.2, high phospholipase activity, bactericidal effect, moderate
cytotoxic activity and was able to inhibit platelet aggregation. Moreover, BmooPLA2 induced moderate
in vivo edema and hypotensive effect. The 414 bp cDNA encoding the BmooPLA2 was cloned and expressed
in Escherichia coli. The recombinant BmooPLA2 showed phospholipase and inhibitory activities on platelet
aggregation similar to those of the native protein. A comparative study between BmooPLA2, the acidic
(BthA-I) and basic (BthTX-II) PLA2 from B. jararacussu venom showed that the effects of BmooPLA2 and
BthA-I-PLA2 are similar. BmooPLA2 is the first isolated and characterized non-myotoxic PLA2 from B.
moojeni snake venom. The recombinant PLA2 can substitute the native toxin in studies aiming its biotechnological
application in order to help the preservation of this endangered species. These data along with
the preliminary structural studies here reported will provide a better understanding of this important
class of proteins.
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