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Extraction of Venom and Venom Gland Microdissections from Spiders for Proteomic and Transcriptomic Analyses
Published on: November 3, 2014
Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation
Ana M Moura-da-Silva1, Michelle T Almeida2, José A Portes-Junior3
1Laboratório de Imunopatologia, Instituto Butantan, São Paulo CEP 05503-900, Brazil. ana.moura@butantan.gov.br.
Abstract:
Snake venom metalloproteinases (SVMPs) are abundant in the venoms of vipers and rattlesnakes, playing important roles for the snake adaptation to different environments, and are related to most of the pathological effects of these venoms in human victims. The effectiveness of SVMPs is greatly due to their functional diversity, targeting important physiological proteins or receptors in different tissues and in the coagulation system. Functional diversity is often related to the genetic diversification of the snake venom. In this review, we discuss some published evidence that posit that processing and post-translational modifications are great contributors for the generation of functional diversity and for maintaining latency or inactivation of enzymes belonging to this relevant family of venom toxins.
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