Comparative proteomic profiling and functional characterization of venom pooled from captive Crotalus durissus terrificus specimens and the Brazilian crotalic reference venom.
Brazilian crotalic reference venom
Crotalus durissus terrificus venom
Snake venomics
Venom of wild caught versus captive snake
Journal
Toxicon : official journal of the International Society on Toxinology
ISSN: 1879-3150
Titre abrégé: Toxicon
Pays: England
ID NLM: 1307333
Informations de publication
Date de publication:
15 Oct 2020
15 Oct 2020
Historique:
received:
19
05
2020
revised:
26
06
2020
accepted:
02
07
2020
pubmed:
8
7
2020
medline:
10
9
2020
entrez:
8
7
2020
Statut:
ppublish
Résumé
The South American rattlesnake Crotalus durissus spp has a wide geographic distribution in Brazil. Although responsible for only a low proportion of ophidian accidents, it is considered one of the most medically important species of venomous snakes due to the high mortality rate (1.87%). Snake venom is a complex phenotype commonly subjected to individual intraspecific, ontogenetic and geographic variability. Compositional differences in pooled venom used in the immunization process may impact the efficacy of the antivenom. In order to assure standardized high-quality antivenom, the potency of each Brazilian crotalic antivenom batch is determined against the 'Brazilian Crotalic Reference Venom' (BCRV). BCRV is produced by Instituto Butantan using venom obtained from the first milking of recently wild-caught C. d. terrificus specimens brought to the Institute. The decrease in the number of snake donations experienced in recent years can become a threat to the production of future batches of BCRV. To evaluate the feasibility of using venom from long-term captive animals in the formulation of BCRV, we have compared the proteomic, biochemical and biological profiles of C. d. terrificus venom pooled from captive specimens (CVP- captive venom pool) and BCRV. Electrophoretic and venomics analyses revealed a very similar venom composition profile, but also certain differences in toxins abundance, with some low abundant protein families found only in BCRV. Enzymatic (L-amino acid oxidase, phospholipase A
Identifiants
pubmed: 32634448
pii: S0041-0101(20)30305-6
doi: 10.1016/j.toxicon.2020.07.001
pii:
doi:
Substances chimiques
Crotalid Venoms
0
Phospholipases A2
EC 3.1.1.4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
26-35Informations de copyright
Copyright © 2020. Published by Elsevier Ltd.