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Functional Variability of Snake Venom Metalloproteinases: Adaptive Advantages in Targeting Different Prey and Implications for Human Envenomation

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Autor(es):
Bernardoni, Juliana L. [1] ; Sousa, Leijiane F. [1] ; Wermelinger, Luciana S. [2, 3] ; Lopes, Aline S. [4, 5] ; Prezoto, Benedito C. [6] ; Serrano, Solange M. T. [4, 5] ; Zingali, Russolina B. [2] ; Moura-da-Silva, Ana M. [1]
Número total de Autores: 8
Afiliação do(s) autor(es):
[1] Inst Butantan, Lab Imunopatol, Sao Paulo - Brazil
[2] Univ Fed Rio de Janeiro, Inst Bioquim Med, Lab Hemostasia & Venenos, Rio Do Janeiro, RJ - Brazil
[3] Univ Fed Rio de Janeiro, Fac Farm, Lab Fisiopatol Trombose, Rio Do Janeiro, RJ - Brazil
[4] Inst Butantan, Lab Especial Toxinol Aplicada, Sao Paulo - Brazil
[5] FAPESP, Ctr Toxins Immune Response & Cell Signaling CeTIC, Sao Paulo - Brazil
[6] Inst Butantan, Farmacol Lab, Sao Paulo - Brazil
Número total de Afiliações: 6
Tipo de documento: Artigo Científico
Fonte: PLoS One; v. 9, n. 10 OCT 14 2014.
Citações Web of Science: 23
Resumo

Snake venom metalloproteinases (SVMPs) are major components in most viperid venoms that induce disturbances in the hemostatic system and tissues of animals envenomated by snakes. These disturbances are involved in human pathology of snake bites and appear to be essential for the capture and digestion of snake's prey and avoidance of predators. SVMPs are a versatile family of venom toxins acting on different hemostatic targets which are present in venoms in distinct structural forms. However, the reason why a large number of different SVMPs are expressed in some venoms is still unclear. In this study, we evaluated the interference of five isolated SVMPs in blood coagulation of humans, birds and small rodents. P-III class SVMPs (fractions Ic, IIb and IIc) possess gelatinolytic and hemorrhagic activities, and, of these, two also show fibrinolytic activity. P-I class SVMPs (fractions IVa and IVb) are only fibrinolytic. P-III class SVMPs reduced clotting time of human plasma. Fraction IIc was characterized as prothrombin activator and fraction Ic as factor X activator. In the absence of Ca2+, a firm clot was observed in chicken blood samples with fractions Ic, IIb and partially with fraction IIc. In contrast, without Ca2+, only fraction IIc was able to induce a firm clot in rat blood. In conclusion, functionally distinct forms of SVMPs were found in B. neuwiedi venom that affect distinct mechanisms in the coagulation system of humans, birds and small rodents. Distinct SVMPs appear to be more specialized to rat or chicken blood, strengthening the current hypothesis that toxin diversity enhances the possibilities of the snakes for hunting different prey or evading different predators. This functional diversity also impacts the complexity of human envenoming since different hemostatic mechanisms will be targeted by SVMPs accounting for the complexity of the response of humans to venoms. (AU)

Processo FAPESP: 12/23018-0 - Vantagens adaptativas da presença de diferentes metaloproteinases na composição dos venenos botrópicos e implicações dessa variabilidade nos acidentes ofídicos
Beneficiário:Juliana Lech Bernardoni
Linha de fomento: Bolsas no Brasil - Doutorado
Processo FAPESP: 12/16277-9 - Variabilidade na composição dos venenos botrópicos e implicações funcionais da presença de diferentes metaloproteinases na composição dos mesmos
Beneficiário:Ana Maria Moura da Silva
Linha de fomento: Auxílio à Pesquisa - Regular