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  4. Caracterización bioquímica del veneno de la serpiente Bothrops roedingeri Mertens, 1942, y sus actividades edematógena, hemorrágica y miotóxica

Caracterización bioquímica del veneno de la serpiente Bothrops roedingeri Mertens, 1942, y sus actividades edematógena, hemorrágica y miotóxica

Author(s)
Oswaldo Nina-Cueva
Derly Yerson Olazabal-Chambilla
Jair Quispe-Arpasi
Adell Alzamora-Sánchez
Mauricio Gomes-Heleno
Date Issued
2 de diciembre de 2020
Type
Article
Volume
40
Issue
4
Start Page
682
End Page
692
DOI
10.7705/biomedica.5228
Abstract
Introduction: Snakebite envenoming is considered by the World Health Organization (WHO) as a neglected tropical disease. Currently, Bothrops snake venoms are being studied intensively, but there is little knowledge about Bothrops roedingeri venom. Objectives: To biochemically characterize B. roedingeri total venom and evaluate its myotoxic, edematogenic, and hemorrhagic activity. Materials and methods: We characterized B. roedingeri venom enzymatic activity by determining the phospholipase A2 and the proteolytic and fibrinogenolytic action using SDSPAGE electrophoresis while we characterized its venom toxicity by determining the minimum hemorrhagic dose, the minimum edema dose, and the local and systemic myotoxic effects. Results: Bothrops roedingeri venom showed a PLA2 activity of 3.45 ± 0.11 nmoles/min, proteolytic activity of 0.145 ± 0.009 nmoles/min, and a fibrinogen coagulation index of 6.67 ± 1.33 seconds. On the other hand, it produced an minimum hemorrhagic dose of 24.5 μg, an minimum edema dose of 15.6 μg, and a pronounced local myotoxic effect evidenced by the elevation of plasma creatine kinase levels after intramuscular inoculation. The venom showed no systemic myotoxicity. Conclusions: Bothrops roedingeri venom has local hemorrhagic, edematogenic, and myotoxic activity. Enzymatically, it has high PLA2 activity, which would be responsible for the myotoxic and edematogenic effects. It also has proteolytic activity, which could affect coagulation given its ability to degrade fibrinogen, and it causes bleeding through the metalloproteases.
Subjects

Humanities

Molecular biology

Art

Biology

Humanities

Molecular biology

Art

Biology

Myotoxicity etiology

Myotoxicity etiology

Myotoxicity etiology

Myotoxicity etiology

Animals

Animals

Animals

Animals

Blood Coagulation Dis...

Blood Coagulation Dis...

Blood Coagulation Dis...

Blood Coagulation Dis...

Creatine Kinase blood...

Creatine Kinase blood...

Creatine Kinase blood...

Creatine Kinase blood...

Crotalid Venoms enzym...

Crotalid Venoms enzym...

Crotalid Venoms enzym...

Crotalid Venoms enzym...

Crotalid Venoms poiso...

Crotalid Venoms poiso...

Crotalid Venoms poiso...

Crotalid Venoms poiso...

Edema chemically indu...

Edema chemically indu...

Edema chemically indu...

Edema chemically indu...

Electrophoresis, Poly...

Electrophoresis, Poly...

Electrophoresis, Poly...

Electrophoresis, Poly...

Female

Female

Female

Female

Hemorrhage chemically...

Hemorrhage chemically...

Hemorrhage chemically...

Hemorrhage chemically...

Male

Male

Male

Male

Mice, Inbred BALB C

Mice, Inbred BALB C

Mice, Inbred BALB C

Mice, Inbred BALB C

Snake Bites

Snake Bites

Snake Bites

Snake Bites

Bothrops

Bothrops

Bothrops

Bothrops

Mice

Mice

Mice

Mice

Phospholipases A2 tox...

Phospholipases A2 tox...

Phospholipases A2 tox...

Phospholipases A2 tox...

Neglected Diseases

Neglected Diseases

Neglected Diseases

Neglected Diseases

Proteolysis

Proteolysis

Proteolysis

Proteolysis

Life Sciences Biochem...

Physical Sciences Ear...

Metrics
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