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Toxins 2017, 9(11), 342; https://doi.org/10.3390/toxins9110342

Isolation and Functional Characterization of an Acidic Myotoxic Phospholipase A2 from Colombian Bothrops asper Venom

1
Programa de Ofidismo y Escorpionismo, Universidad de Antioquia, Medellín 050010, Colombia
2
Research Group in Veterinary Medicine GIVET, School of Veterinary Medicine, Corporación Universitaria Lasallista, Caldas-Antioquia 055440, Colombia
3
Grupo de Inmunología Celular e Inmunogenética (GICIG), Universidad de Antioquia, Medellín 050010, Colombia
4
Center for the Study of Venoms and Venomous Animals (CEVAP), Universidad Estadual Paulista (UNESP) and Graduate Program in Tropical Diseases, Botucatu Medical School (FMB), Botucatu, São Paulo 18610-307, Brazil
5
Escuela de Microbiología, Universidad de Antioquia, Medellín 050010, Colombia
*
Author to whom correspondence should be addressed.
Academic Editors: Stuart M. Brierley and Irina Vetter
Received: 12 September 2017 / Revised: 10 October 2017 / Accepted: 11 October 2017 / Published: 26 October 2017
(This article belongs to the Section Animal Venoms)
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Abstract

Myotoxic phospholipases A2 (PLA2) are responsible for many clinical manifestations in envenomation by Bothrops snakes. A new myotoxic acidic Asp49 PLA2 (BaCol PLA2) was isolated from Colombian Bothrops asper venom using reverse-phase high performance liquid chromatography (RP-HPLC). BaCol PLA2 had a molecular mass of 14,180.69 Da (by mass spectrometry) and an isoelectric point of 4.4. The complete amino acid sequence was obtained by cDNA cloning (GenBank accession No. MF319968) and revealed a mature product of 124 amino acids with Asp at position 49. BaCol PLA2 showed structural homology with other acidic PLA2 isolated from Bothrops venoms, including a non-myotoxic PLA2 from Costa Rican B. asper. In vitro studies showed cell membrane damage without exposure of phosphatidylserine, an early apoptosis hallmark. BaCol PLA2 had high indirect hemolytic activity and moderate anticoagulant action. In mice, BaCol PLA2 caused marked edema and myotoxicity, the latter seen as an increase in plasma creatine kinase and histological damage to gastrocnemius muscle fibers that included vacuolization and hyalinization necrosis of the sarcoplasm. View Full-Text
Keywords: acidic myotoxic phospholipase A2; Bothrops asper; edema; myotoxicity; snake venom acidic myotoxic phospholipase A2; Bothrops asper; edema; myotoxicity; snake venom
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Posada Arias, S.; Rey-Suárez, P.; Pereáñez J, A.; Acosta, C.; Rojas, M.; Delazari dos Santos, L.; Ferreira Jr, R.S.; Núñez, V. Isolation and Functional Characterization of an Acidic Myotoxic Phospholipase A2 from Colombian Bothrops asper Venom. Toxins 2017, 9, 342.

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