Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia

ABSTRACT: Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panama, Colombia, and Ecuador, whose venom is poorly characterized. In the ́ present work, the protein composition of this venom was profiled using the ‘snake venomics’ analytical strategy. Decomplexation of...

Full description

Autores:
Fernández Culma, Maritza
Pereañez Jiménez, Jaime Andrés
Núñez Rangel, Vitelbina
Lomonte, Bruno
Tipo de recurso:
Article of investigation
Fecha de publicación:
2014
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/36220
Acceso en línea:
https://hdl.handle.net/10495/36220
Palabra clave:
Venenos de Serpiente
Snake Venoms
Viperidae
Proteómica
Proteomics
Colombia
Ecuador
Panamá
Mordeduras de Serpientes
Snake Bites
Bothrops punctatus
Rights
openAccess
License
https://creativecommons.org/licenses/by/4.0/
Description
Summary:ABSTRACT: Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panama, Colombia, and Ecuador, whose venom is poorly characterized. In the ́ present work, the protein composition of this venom was profiled using the ‘snake venomics’ analytical strategy. Decomplexation of the crude venom by RP-HPLC and SDS-PAGE, followed by tandem mass spectrometry of tryptic digests, showed that it consists of proteins assigned to at least nine snake toxin families. Metalloproteinases are predominant in this secretion (41.5% of the total proteins), followed by C-type lectin/lectin-like proteins (16.7%), bradykinin-potentiating peptides (10.7%), phospholipases A2 (9.3%), serine proteinases (5.4%), disintegrins (3.8%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (1.7%), and cysteine-rich secretory proteins (1.2%). Altogether, 6.6% of the proteins were not identified. In vitro, the venom exhibited proteolytic, phospholipase A2, and L-amino acid oxidase activities, as well as angiotensin-converting enzyme (ACE)-inhibitory activity, in agreement with the obtained proteomic profile. Cytotoxic activity on murine C2C12 myoblasts was negative, suggesting that the majority of venom phospholipases A2 likely belong to the acidic type, which often lack major toxic effects. The protein composition of B. punctatus venom shows a good correlation with toxic activities here and previously reported, and adds further data in support of the wide diversity of strategies that have evolved in snake venoms to subdue prey, as increasingly being revealed by proteomic analyses.