Comparison of venoms from wild and long-term captive Bothrops atrox snakes and characterization of Batroxrhagin, the predominant class PIII metalloproteinase from the venom of this species

Comparison of venoms from wild and long-term captive Bothrops atrox snakes and characterization of Batroxrhagin, the predominant class PIII metalloproteinase from the venom of this species

Comparisons between venoms from snakes kept under captivity or collected at the natural environment are of fundamental importance in order to obtain effective antivenoms to treat human victims of snakebites. In this study, we compared composition and biological activities of Bothrops atrox venom fro...

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Bibliographic Details
Published in:Biochimie Vol. 118; pp. 60 - 70
Main Authors: Freitas-de-Sousa, L.A., Amazonas, D.R., Sousa, L.F., Sant'Anna, S.S., Nishiyama, M.Y., Serrano, S.M.T., Junqueira-de-Azevedo, I.L.M., Chalkidis, H.M., Moura-da-Silva, A.M., Mourão, R.H.V.
Format: Journal Article
Language:English
Published: France Elsevier B.V 01-11-2015
Subjects:
Amino Acid Sequence
Animals
Antivenom
Bothrops - physiology
Bothrops atrox
Chromatography, High Pressure Liquid
Chromatography, Liquid
Crotalid Venoms - chemistry
Crotalid Venoms - metabolism
Female
Hemorrhage
Male
Metalloproteases - chemistry
Metalloproteases - metabolism
Metalloproteinase
Molecular Sequence Data
RNA, Messenger - analysis
Snake venom
Tandem Mass Spectrometry
Venom variability
SVMP
Snake venom
Antivenom
Bothrops atrox
Venom variability
SVSP
PLA2
Metalloproteinase
Hemorrhage
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Summary:Comparisons between venoms from snakes kept under captivity or collected at the natural environment are of fundamental importance in order to obtain effective antivenoms to treat human victims of snakebites. In this study, we compared composition and biological activities of Bothrops atrox venom from snakes collected at Tapajós National Forest (Pará State, Brazil) or maintained for more than 10 years under captivity at Instituto Butantan herpetarium after have been collected mostly at Maranhão State, Brazil. Venoms from captive or wild snakes were similar except for small quantitative differences detected in peaks correspondent to phospholipases A2 (PLA2), snake venom metalloproteinases (SVMP) class PI and serine proteinases (SVSP), which did not correlate with fibrinolytic and coagulant activities (induced by PI-SVMPs and SVSPs). In both pools, the major toxic component corresponded to PIII-SVMPs, which were isolated and characterized. The characterization by mass spectrometry of both samples identified peptides that matched with a single PIII-SVMP cDNA characterized by transcriptomics, named Batroxrhagin. Sequence alignments show a strong similarity between Batroxrhagin and Jararhagin (96%). Batroxrhagin samples isolated from venoms of wild or captive snakes were not pro-coagulant, but inhibited collagen-induced platelet-aggregation, and induced hemorrhage and fibrin lysis with similar doses. Results suggest that in spite of environmental differences, venom variability was detected only among the less abundant components. In opposition, the most abundant toxin, which is a PIII-SVMP related to the key effects of the venom, is structurally conserved in the venoms. This observation is relevant for explaining the efficacy of antivenoms produced with venoms from captive snakes in human accidents inflicted at distinct natural environments. •Bothrops atrox venom from Brazilian wild snakes or kept under captivity were compared.•Variability in protein composition was observed only in the less abundant components.•Differences in venom composition did not correlate to major venom functions.•Venoms shared the same major toxin: Bathoxrhagin, a hemorrhagic metalloproteinase.
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ISSN:0300-9084
1638-6183
DOI:10.1016/j.biochi.2015.08.006