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

Author(s)

Freitas-de-Sousa, L. A. ^{[1, 2]} ; Amazonas, D. R. ^[1] ; Sousa, L. F. ^[1] ; Sant'Anna, S. S. ^[3] ; Nishiyama, Jr., M. Y. ^[4] ; Serrano, S. M. T. ^[4] ; Junqueira-de-Azevedo, I. L. M. ^[4] ; Chalkidis, H. M. ^[5] ; Moura-da-Silva, A. M. ^[1] ; Mourao, R. H. V. ^[2]

Affiliation

^[1] Inst Butantan, Lab Imunopatol, BR-05503900 Sao Paulo, SP - Brazil

^[2] Univ Fed Oeste Para UFOPA, Lab Bioprospeccao & Biol Expt, Programa Posgrad Recursos Nat Amazonia, BR-68035110 Santarem, PA - Brazil

^[3] Inst Butantan, Lab Herpetol, BR-05503900 Sao Paulo, SP - Brazil

^[4] Inst Butantan, Lab Especial Toxinol Aplicada, BR-05503900 Sao Paulo, SP - Brazil

^[5] FIT, BR-68010200 Santarem, PA - Brazil

• Document type: Review article
• Source: Biochimie; v. 118, p. 60-70, NOV 2015.
• Web of Science Citations: 25

Abstract

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 Tapajos National Forest (Para State, Brazil) or maintained for more than 10 years under captivity at Instituto Butantan herpetarium after have been collected mostly at Maranhao State, Brazil. Venoms from captive or wild snakes were similar except for small quantitative differences detected in peaks correspondent to phospholipases A(2) (PIA(2)), 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. (C) 2015 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. (AU)

• FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
• Grantee: Hugo Aguirre Armelin
• Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC
• FAPESP's process: 12/16277-9 - Variability in venom composition of Bothrops snakes and functional relevance of the presence of distinct metaloproteinases in venom composition
• Grantee: Ana Maria Moura da Silva
• Support Opportunities: Regular Research Grants
• FAPESP's process: 14/26058-8 - Inhibition of mammalian and snake venom metalloproteinases by the recombinant pro-domain of jararhagin and its relevant peptide fragments
• Grantee: Ana Maria Moura da Silva
• Support Opportunities: Regular Research Grants