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EXPLORING AND UNDERSTANDING THE FUNCTIONAL ROLE, AND BIOCHEMICAL AND STRUCTURAL CHARACTERISTICS OF AN ACIDIC PHOSPHOLIPASE A2, APLTX-I, PURIFIED FROM AGKISTRODON PISCIVORUS LEUCOSTOMA SNAKE VENOM
Snake venom
Agkistrodon piscivorus leucostoma
Pharmacological activity
Autor
Afiliación
Campinas State University. Institute of Biology. Department of Biochemistry and Tissue Biology. Campinas, SP, Brasil.
Universidad Regional Amazônica. Tena, Napo, Ecuador. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
State University of Campinas. Faculty of Medical Sciences. Department of Pharmacology. Campinas, SP, Brasil.
State University of Campinas. Faculty of Medical Sciences. Department of Pharmacology. Campinas, SP, Brasil.
State University of Campinas. Faculty of Medical Sciences. Department of Pharmacology. Campinas, SP, Brasil.
Universidad de Talca. Centro de Bioinformática y Simulación Molecular. Talca, Chile.
Universidad de Talca. Centro de Bioinformática y Simulación Molecular. Talca, Chile. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas. Federal University of Rondônia. Porto Velho, RO, Brasil. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas. Federal University of Rondônia. Porto Velho, RO, Brasil. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
Campinas State University. Institute of Biology. Department of Biochemistry and Tissue Biology. Campinas, SP, Brasil.
Universidad Regional Amazônica. Tena, Napo, Ecuador. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
Universidad Regional Amazônica. Tena, Napo, Ecuador. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
State University of Campinas. Faculty of Medical Sciences. Department of Pharmacology. Campinas, SP, Brasil.
State University of Campinas. Faculty of Medical Sciences. Department of Pharmacology. Campinas, SP, Brasil.
State University of Campinas. Faculty of Medical Sciences. Department of Pharmacology. Campinas, SP, Brasil.
Universidad de Talca. Centro de Bioinformática y Simulación Molecular. Talca, Chile.
Universidad de Talca. Centro de Bioinformática y Simulación Molecular. Talca, Chile. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas. Federal University of Rondônia. Porto Velho, RO, Brasil. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
Fundação Oswaldo Cruz. Centro de Estudos de Biomoléculas. Federal University of Rondônia. Porto Velho, RO, Brasil. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
Campinas State University. Institute of Biology. Department of Biochemistry and Tissue Biology. Campinas, SP, Brasil.
Universidad Regional Amazônica. Tena, Napo, Ecuador. / International Network of Ecuadorian Snakes Venom Studies. Ecuador.
Resumen en ingles
Phospholipases A2 (PLA2s) constitute a class of extensively studied toxins, isolated from snake venoms. Basic PLA2 isoforms mediate various toxicological effects, while the acidic isoforms generally have higher enzymatic activities, but do not promote evident toxic effects. The functions of these acidic isoforms in snake venoms are still not completely understood and more studies are needed to characterize the biological functions and diversification of acidic toxins in order to justify their abundant presence in these secretions. Recently, Lomonte and collaborators demonstrated, in a proteomic and toxicological study, high concentrations of PLA2s in the venom of Agkistrodon piscivorus leucostoma. We have, herein, purified and characterized an acidic PLA2 from this snake venom, denominated AplTx-I, in order to better understand its biochemical and structural characteristics, as well as its biological effects. AplTx-I was purified using two chromatographic steps, in association with enzymatic and biological assays. The acidic toxin was found to be one of the most abundant proteins in the venom of A. p. leucostoma; the protein was monomeric with a molecular mass of 13,885.8 Da, as identified by mass spectrometry ESI-TOF and electrophoresis. The toxin has similar primary and tridimensional structures to those of other acidic PLA2s, a theoretical and experimental isoelectric point of z5.12, and a calcium-dependent enzyme activity of 25.8985 nM/min/mg, with maximum values at 37 C and pH 8.0. Despite its high enzymatic activity on synthetic substrate, AplTx-I did not induce high or significant myotoxic, coagulant, anticoagulant, edema, neuromuscular toxicity in mouse phrenic nerve-diaphragm
preparations or antibacterial activities. Interestingly, AplTx-I triggered a high and selective neuromuscular toxicity in chick biventer cervicis preparations. These findings are relevant to provide a deeper understanding of the pharmacology, role and diversification of acidic phospholipase A2 isoforms in snake venoms.
Palabras clave en ingles
Acidic phospholipase A2Snake venom
Agkistrodon piscivorus leucostoma
Pharmacological activity
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