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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
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]
Total Authors: 8
Affiliation:
[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
Total Affiliations: 6
Document type: Journal article
Source: PLoS One; v. 9, n. 10 OCT 14 2014.
Web of Science Citations: 21
Abstract

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)

FAPESP's process: 12/16277-9 - Variability in venom composition of Bothrops snakes and functional relevance of the presence of distinct metaloproteinases in venom composition
Grantee:Ana Maria Moura da Silva
Support Opportunities: Regular Research Grants
FAPESP's process: 12/23018-0 - Adaptative advantages of the presence of different metalloproteinases in the composition of Bothrops venoms and implications of this variability in snakebites
Grantee:Juliana Lech Bernardoni
Support Opportunities: Scholarships in Brazil - Doctorate