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

Autor(es)

Moura-da-Silva, Ana M. ^[1] ; Almeida, Michelle T. ^[1] ; Portes-Junior, Jose A. ^[1] ; Nicolau, Carolina A. ^[2] ; Gomes-Neto, Francisco ^[2] ; Valente, Richard H. ^[2]

Afiliação do(s) autor(es)

^[1] Inst Butantan, Lab Imunopatol, BR-05503900 Sao Paulo - Brazil

^[2] Inst Oswaldo Cruz, Lab Toxinol, BR-21040360 Rio De Janeiro - Brazil

• Tipo de documento: Artigo de Revisão
• Fonte: TOXINS; v. 8, n. 6 JUN 2016.
• Citações Web of Science: 10

Resumo

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. (AU)

• Processo FAPESP: 14/26058-8 - Inibição de metaloproteinases de mamíferos e de venenos de serpentes pelo pró-domínio recombinante da jararagina e seus fragmentos peptídicos
• Beneficiário: Ana Maria Moura da Silva
• Modalidade de apoio: Auxílio à Pesquisa - Regular