A novel pentameric phospholipase A 2 myotoxin (PophPLA 2 ) from the venom of the pit viper Porthidium ophryomegas

The first toxin isolated from the venomous pit viper Porthidium ophryomegas is a basic pentameric phospholipase A (PophPLA ). Elucidation of its amino acid sequence showed that it belongs to the group IIA of secreted PLA s, with the presence of all 14 conserved cysteine positions. The toxin displaye...

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Bibliographic Details
Published in:International journal of biological macromolecules 2018-10, Vol.118 (Pt A), p.1
Main Authors: Vindas, Julio, Carrera, Yarina, Lomonte, Bruno, Gutiérrez, José María, Calvete, Juan J, Sanz, Libia, Fernández, Julián
Format: Article
Language:English
Subjects:
Amino Acid Sequence - genetics
Animals
Crotalid Venoms - chemistry
Crotalid Venoms - enzymology
Crotalid Venoms - genetics
Crotalid Venoms - pharmacology
Crotalinae
Humans
Mice
Phospholipases A2 - chemistry
Phospholipases A2 - genetics
Phospholipases A2 - pharmacology
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Summary:The first toxin isolated from the venomous pit viper Porthidium ophryomegas is a basic pentameric phospholipase A (PophPLA ). Elucidation of its amino acid sequence showed that it belongs to the group IIA of secreted PLA s, with the presence of all 14 conserved cysteine positions. The toxin displayed catalytic activity, in agreement with the presence of Asp49 in its sequence of 121 residues. SDS-PAGE analysis revealed that this toxin is pentameric in non-reducing conditions, a structural organization that has not been described for any viperid PLA . PophPLA displayed moderate myotoxic (in vivo) and cytotoxic (in vitro) activities, as well as anticoagulant activity on human plasma (in vitro). PophPLA was not lethal, and did not induce signs of toxicity or distress in mice, when administered intravenously at a dose of up to 100 μg (5.9 μg/g). The toxin showed highest sequence identity with other PLA s from the venoms of ancestral Asian pit viper species.
ISSN:1879-0003
DOI:10.1016/j.ijbiomac.2018.06.028