Proteomic profiling, functional characterization, and immunoneutralization of the venom of Porthidium porrasi, a pitviper endemic to Costa Rica

 

Guardado en:
Detalles Bibliográficos
Autores: Méndez Argüello, Rebeca, Bonilla Murillo, Fabián, Sasa Marín, Mahmood, Dwyer, Quetzal, Fernández Ulate, Julián, Lomonte, Bruno
Formato: artículo original
Fecha de Publicación:2019
Descripción:The genus Porthidium includes nine pitviper species inhabiting Mexico, Central America, and northern South America. Porthidium porrasi is a species endemic to the Southwest of Costa Rica, for which no information on its venom was available. In this study, the proteomic composition and functional activities of P. porrasi venom are described. The most abundant venom proteins were identified as metalloproteinases (36.5%). In descending order of abundance, proteins belonging to the disintegrin, phospholipase A2, serine proteinase, C-type lectin/ lectin-like, vascular endothelial growth factor, Cysteine-rich secretory protein, L-amino acid oxidase, phospholipase B, and phosphodiesterase families were also identified. P. porrasi venom showed a weak lethal potency in mice (10 μg/g body weight by intraperitoneal route), induced marked hemorrhage and edema, and weak myotoxic effect. These in vivo activities, as well as those assayed in vitro (proteolytic and phospholipase A2 activities) correlated with compositional data. A comparison of P. porrasi venom with those of three other Porthidium species studied to date reveals a generally conserved compositional and functional pattern in this pitviper genus. Importantly, the lethal effect of P. porrasi venom in mice was adequately cross-neutralized by a heterospecific polyvalent antivenom, supporting its use in the treatment of eventual envenomings by this species.
País:Kérwá
Institución:Universidad de Costa Rica
Repositorio:Kérwá
OAI Identifier:oai:https://www.kerwa.ucr.ac.cr:10669/80367
Acceso en línea:https://www.sciencedirect.com/science/article/abs/pii/S0001706X19301056?via%3Dihub
https://hdl.handle.net/10669/80367
Access Level:acceso abierto
Palabra clave:Snake venom
Porthidium porrasi
Pitviper
Venomics
Proteome
Toxicity
Neutralization