Characterization of a basic phospholipase A2-homologeu myotoxin isolated from the venom of the snake Bothrops neuwiedii (yarará chica) from Argentina

• Autores: Geoghegan, Patricia A.; Angulo, Yamileth; Cangelosi, Adriana; Díaz, Mónica; Lomonte, Bruno
• Año de publicación: 1999
• Idioma: inglés
• Tipo de recurso: artículo
• Materia: Venenos de Serpiente; Argentina; Fosfolipasas A2; Edema; Bothrops
• Institución: Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"

Fil: Geoghegan, Patricia A. ANLIS Dr.C.G.Malbrán. Centro Nacional de Control de Calidad de Biológicos. Servicio de Inmunoterapéuticos; Argentina.
Fil: Angulo, Yamileth. Universidad de Costa Rica. Facultad de Microbiología. Instituto Clodomiro Picado; Costa Rica.
Fil: Cangelosi, Adriana. ANLIS Dr.C.G.Malbrán. Centro Nacional de Control de Calidad de Biológicos. Servicio de Inmunoterapéuticos; Argentina.
Fil: Díaz, Mónica. ANLIS Dr.C.G.Malbrán. Centro Nacional de Control de Calidad de Biológicos. Servicio de Inmunoterapéuticos; Argentina.
Fil: Lomonte, Bruno. Universidad de Costa Rica. Facultad de Microbiología. Instituto Clodomiro Picado; Costa Rica.
A basic protein was isolated by CM-Sephadex C-25 chromatography from the venom of Bothrops neuwiedii from Argentina, and named B. neuwiedii myotoxin I. This protein exerted local myotoxic and edema-forming effects in mice, with potencies comparable to other myotoxins isolated from Bothrops spp. venoms. When injected by i.v. route at doses up to 4.7 mg/kg of body weight, the toxin was not lethal. In vitro, the toxin had no detectable phospholipase A2 activity on egg yolk phospholipids. B. neuwiedii myotoxin I appeared as a homodimer in sodium dodecylsulphate-polyacrylamide gel electrophoresis, with a subunit molecular weight of 15 kD. Gel immunodiffusion revealed a pattern of partial antigenic identity between the newly isolated myotoxin and myotoxin II from Bothrops asper venom. The sequence of B. neuwiedii myotoxin I was determined for the first 40 amino acid residues, showing high homology to several class II phospholipase A2 myotoxins of the Lys-49 family from crotalids. Altogether, results suggest that this toxin is a new member of the Lys-49 phospholipase A2-homologues with myotoxic, cytolytic, and edema-inducing activities.