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Toxins 2016, 8(6), 183; doi:10.3390/toxins8060183

Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation

1
Laboratório de Imunopatologia, Instituto Butantan, São Paulo CEP 05503-900, Brazil
2
Laboratório de Toxinologia, Instituto Oswaldo Cruz, Rio de Janeiro CEP 21040-360, Brazil
*
Author to whom correspondence should be addressed.
Academic Editors: Jay Fox and José María Gutiérrez
Received: 4 May 2016 / Revised: 27 May 2016 / Accepted: 3 June 2016 / Published: 9 June 2016
(This article belongs to the Special Issue Snake Venom Metalloproteinases)
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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. View Full-Text
Keywords: snake venom; metalloproteinase; post-translational processing; enzyme inhibitor; hemorrhage snake venom; metalloproteinase; post-translational processing; enzyme inhibitor; hemorrhage
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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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MDPI and ACS Style

Moura-da-Silva, A.M.; Almeida, M.T.; Portes-Junior, J.A.; Nicolau, C.A.; Gomes-Neto, F.; Valente, R.H. Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation. Toxins 2016, 8, 183.

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