Venom of the crotaline snake Atropoides nummifer (jumping viper) from Guatemala and Honduras: comparative toxicological characterization, isolation of a myotoxic phospholipase A(2) homologue and neutralization by two antivenoms
Autor: | Patricia Saravia, Yamileth Angulo, Rubén Velásquez, Bruno Lomonte, Ermila Rojas, José María Gutiérrez, Monica Thelestam, Viviana Arce, Juan José Chávez |
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Jazyk: | angličtina |
Rok vydání: | 2001 |
Předmět: |
Snake venom
Injections Intradermal Physiology Health Toxicology and Mutagenesis Myotoxin Antivenom Venom Hemorrhage Cross Reactions In Vitro Techniques Toxicology Biochemistry complex mixtures Injections Intramuscular Phospholipases A Microbiology Lethal Dose 50 Mice Viperidae Atropoides Neutralization Tests biology.animal Atropoides nummifer Crotalid Venoms Animals Edema Amino Acid Sequence Muscle Skeletal Cells Cultured Chromatography High Pressure Liquid Phospholipase A Chromatography biology Antivenins Coagulants Fibrinolysis Cell Biology General Medicine biology.organism_classification Chromatography Ion Exchange Guatemala Honduras Electrophoresis Polyacrylamide Gel Injections Intraperitoneal |
Zdroj: | Comparative Biochemistry and Physiology Part C: Toxicology & pharmacology; Volumen 129, Número 2. 2001 Kérwá Universidad de Costa Rica instacron:UCR |
Popis: | A comparative study was performed on the venoms of the crotaline snake Atropoides nummifer from Guatemala and Honduras. SDS-polyacrylamide gel electrophoresis, under reducing conditions, revealed a highly similar pattern of these venoms, and between them and the venom of the same species from Costa Rica. Similar patterns were also observed in ion-exchange chromatography on CM-Shephadex C-25, in which a highly basic myotoxic fraction was present. This fraction was devoid of phospholipase A(2) activity and strongly reacted, by enzyme-immunoassay, with an antiserum against Bothrops asper myotoxin II, a Lys-49 phospholipase A(2) homologue. A basic myotoxin of 16 kDa was isolated to homogeneity from the venom of A. nummifer from Honduras, showing amino acid composition and N-terminal sequence similar to those of Lys-49 phospholipase A(2) variants previously isolated from other crotaline snake venoms. Guatemalan and Honduran A. nummifer venoms have a qualitatively similar toxicological profile, characterized by: lethal; hemorrhagic; myotoxic; edema-forming; coagulant; and defibrinating activities, although there were significant quantitative variations in some of these activities between the two venoms. Neutralization of toxic activities by two commercially-available antivenoms in the region was studied. Polyvalent antivenom produced by Instituto Clodomiro Picado was effective in the neutralization of: lethal; hemorrhagic; myotoxic; coagulant; defibrinating; and phospholipase A(2) activities, but ineffective against edema-forming activity. On the other hand, MYN polyvalent antivenom neutralized: hemorrhagic; myotoxic; coagulant; defibrinating; and phospholipase A(2) activities, albeit with a lower potency than Instituto Clodomiro Picado antivenom. MYN antivenom failed to neutralize lethal and edema-forming activities of A. nummifer venoms. Universidad de Costa Rica/[741-99-269]/UCR/Costa Rica Universidad de Costa Rica/[741-89-057]/UCR/Costa Rica Network for Research and Training in Tropical Diseases in Central America//NeTropica/ International Foundation for Science/[2677-1]/IFS/Suecia Consejo Nacional de Ciencia y Tecnología/[MS-058-1]/CONICYT/Guatemala UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) |
Databáze: | OpenAIRE |
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