Combined snake venomics and venom gland transcriptomic analysis of Bothropoides pauloensis

Rodrigues, Renata Santos; Boldrini-França, Johara; Fonseca, Fernando P.P.; Torre, Pilar de la; Henrique-Silva, Flávio; Sanz, Libia; Calvete, Juan J.; Rodrigues, Veridiana M.

doi:10.1016/j.jprot.2012.03.028

Cited by 73 publications

(57 citation statements)

References 74 publications

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“…This method is used in several venomics studies [15,16,20,49,50], what allows the inference of protein composition in each chromatographic peak by comparison with proteomic data available in the literature. Our results show a great similarity in the chromatographic profile of B. atrox venom from wild and captive snakes except for quantitative differences in the area of small peaks eluted at the same positions as K-49 PLA 2 , D-49 PLA 2 , PI-SVMPs and SVSPs, higher in venoms of wild snakes, suggesting that the expression of these proteins, although in lower concentrations in the venom, suffer the greatest effect environmental changes.…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2015

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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.

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Section: Discussionmentioning

confidence: 99%

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

et al. 2015

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“…This is one of the reasons why these enzymes may not be detected in transcriptomic and proteomic analyses. It was found only truncated hyaluronidases in the cDNA libraries of Echis carinatus sochureki (Harrison et al, 2007), Bothrops alternatus (Cardoso et al, 2010) and B. neuwiedi pauloensis (Rodrigues et al, 2012). …”

Section: Discussionmentioning

confidence: 99%

Identification of hyaluronidase and phospholipase B in Lachesis muta rhombeata venom

Wiezel

Santos

Cordeiro

et al. 2015

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Hyaluronidases contribute to local and systemic damages after envenoming, since they act as spreading factors cleaving the hyaluronan presents in the connective tissues of the victim, facilitating the diffusion of venom components. Although hyaluronidases are ubiquitous in snake venoms, they still have not been detected in transcriptomic analysis of the Lachesis venom gland and neither in the proteome of its venom performed previously. This work purified a hyaluronidase from Lachesis muta rhombeata venom whose molecular mass was estimated by SDS-PAGE to be 60 kDa. The hyaluronidase was more active at pH 6 and 37 °C when salt concentration was kept constant and more active in the presence of 0.15 M monovalent ions when the pH was kept at 6. Venom was fractionated by reversed-phase liquid chromatography (RPLC). Edman sequencing after RPLC failed to detect hyaluronidase, but identified a new serine proteinase isoform. The hyaluronidase was identified by mass spectrometry analysis of the protein bands in SDS-PAGE. Additionally, phospholipase B was identified for the first time in Lachesis genus venom. The discovery of new bioactive molecules might contribute to the design of novel drugs and biotechnology products as well as to development of more effective treatments against the envenoming.

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“…Cloning-based transcriptomes have been produced even recently (Rodrigues et al, 2012) for Bothropoides pauloensis, and this technique is still a viable alternative to NGS, because it is relatively inexpensive to produce 1000 to 2000 sequences and only requires equipment and reagents readily available in molecular biology laboratories. The first use of NGS for cataloging toxin genes from venom glands was done fairly recently using 454 technology to catalog toxins from the eastern diamondback rattlesnake (C. adamanteus) (Rokyta et al, 2011).…”

Section: A Brief History Of Venom Gland Transcriptomicsmentioning

confidence: 99%

Venom gland transcriptomics for identifying, cataloging, and characterizing venom proteins in snakes

Brahma

McCleary

Kini

et al. 2015

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Combined snake venomics and venom gland transcriptomic analysis of Bothropoides pauloensis

Cited by 73 publications

References 74 publications

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

Identification of hyaluronidase and phospholipase B in Lachesis muta rhombeata venom

Venom gland transcriptomics for identifying, cataloging, and characterizing venom proteins in snakes

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