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Biochemical and physiological characterization of a new Na+-channel specific peptide from the venom of the Argentinean scorpion Tityus trivittatus
Institution:1. Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Mexico;2. Laboratorio de Toxinopatología, Centro de Patología Experimental y Aplicada, Facultad de Medicina, Universidad de Buenos Aires and Ministerio de Salud de la Nación, Argentina;1. Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia UdeA, Carrera 53 No. 61-30, Medellín 050010, Colombia;2. Programa de Ofidismo/Escorpionismo, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia UdeA, Carrera 53 No. 61-30, Medellín 050010, Colombia;3. Facultad de Medicina, Universidad Cooperativa de Colombia, Calle 50 A No. 41-20, Medellín 050010, Colombia;4. Departamento de Ciencias, Laboratorio de Biología y Bioinformática, Universidad Iberoamericana de Ciencias y Tecnología, Padre Miguel de Olivares No. 1620, Santiago de Chile, Chile;1. Toxicology and Pharmacology, University of Leuven (KU Leuven), Campus Gasthuisberg, O&N2, PO Box 922, Herestraat 49, 3000 Leuven, Belgium;2. Physics and Chemistry Department, Faculty of Pharmaceutical Sciences, Ribeirão Preto – USP, Ribeirão Preto, SP, Brazil;3. From the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow,;4. the Kamchatka Branch of the Pacific Institute of Geography, Far-Eastern Branch of the Russian Academy of Sciences, ul. Partizanskaya 6, 683000 Petropavlovsk-Kamchatsky, and;5. the Branch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, Moscow, Russia;1. Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of sciences, Kunming 650223, China;2. Graduate University of Chinese Academy of Sciences, Beijing 100009, China;3. Joint Laboratory of Natural peptide, University of Science and Technology of China and Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China;1. Jiangsu Provincial Key Laboratory for TCM Evaluation and Translational Development, China Pharmaceutical University, Nanjing, 211198, PR China;2. College of Chemistry, Beijing Normal University, Beijing, 100875, PR China;1. College of Medicine and Dentistry, Cairns Campus, James Cook University, Cairns, Queensland 4878, Australia;2. Translational Neuroscience Facility and Department of Physiology, School of Medical Sciences, UNSW Australia, Sydney, NSW 2052, Australia;3. Centre for Tropical Environmental and Sustainability Science and College of Science & Engineering, Cairns Campus, James Cook University, Cairns, Queensland 4878, Australia;4. Centre for Biodiscovery and Molecular Development of Therapeutics, James Cook University, Queensland 4878, Australia;5. Australian Institute of Tropical Health and Medicine, James Cook University, Cairns Campus, QLD, Australia
Abstract:A new peptide with 61 amino acids cross-linked by 4 disulfide bridges, with molecular weight of 6938.12 Da, and an amidated C-terminal amino acid residue was purified and characterized. The primary structure was obtained by direct Edman degradation and sequencing its gene. The peptide is lethal to mammals and was shown to be similar (95% identity) to toxin Ts1 (gamma toxin) from the Brazilian scorpion Tityus serrulatus; it was named Tt1g (from T. trivittatus toxin 1 gamma-like). Tt1g was assayed on several sub-types of Na+-channels showing displacement of the currents to more negative voltages, being the hNav1.3 the most affected channel. This toxin displays characteristics typical to the β-type sodium scorpion toxins. Lethality tests and physiological assays indicate that this peptide is probably the most important toxic component of this species of scorpion, known for causing human fatalities in the South American continent.
Keywords:β-Toxin  cDNA cloning  Primary structure  Scorpion
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