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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The absence of thrombin-like activity in Bothrops erythromelas venom is due to the deletion of the snake venom thrombin-like enzyme gene

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Lotto, Nicholas P. [1] ; Modesto, Jeanne C. de Albuquerque [2] ; Sant'Anna, Savio S. [3] ; Grego, Kathleen F. [3] ; Guarnieri, Miriam C. [4] ; Lira-da-Silva, Rejane M. [5] ; Santoro, Marcelo L. [6] ; Oguiura, Nancy [1]
Total Authors: 8
[1] Inst Butantan, Lab Ecol & Evolut, Sao Paulo - Brazil
[2] Univ Fed Pernambuco, Vitoria Acad Ctr, Vitoria, PE - Brazil
[3] Inst Butantan, Lab Herpetol, Sao Paulo - Brazil
[4] Univ Fed Pernambuco, Dept Zool, Recife, PE - Brazil
[5] Univ Fed Bahia, Inst Biol, Salvador, BA - Brazil
[6] Inst Butantan, Lab Pathophysiol, Sao Paulo - Brazil
Total Affiliations: 6
Document type: Journal article
Source: PLoS One; v. 16, n. 4 APR 27 2021.
Web of Science Citations: 0

Snake venom thrombin-like enzymes (SVTLEs) are serine proteinases that clot fibrinogen. SVTLEs are distributed mainly in venoms from snakes of the Viperidae family, comprising venomous pit viper snakes. Bothrops snakes are distributed throughout Central and South American and are responsible for most venomous snakebites. Most Bothrops snakes display thrombin-like activity in their venoms, but it has been shown that some species do not present it. In this work, to understand SVTLE polymorphism in Bothrops snake venoms, we studied individual samples from two species of medical importance in Brazil: Bothrops jararaca, distributed in Southeastern Brazil, which displays coagulant activity on plasma and fibrinogen, and Bothrops erythromelas, found in Northeastern Brazil, which lacks direct fibrinogen coagulant activity but shows plasma coagulant activity. We tested the coagulant activity of venoms and the presence of SVTLE genes by a PCR approach. The SVTLE gene structure in B. jararaca is similar to the Bothrops atrox snake, comprising five exons. We could not amplify SVTLE sequences from B. erythromelas DNA, except for a partial pseudogene. These genes underwent a positive selection in some sites, leading to an amino acid sequence diversification, mostly in exon 2. The phylogenetic tree constructed using SVTLE coding sequences confirms that they are related to the chymotrypsin/kallikrein family. Interestingly, we found a B. jararaca specimen whose venom lacked thrombin-like activity, and its gene sequence was a pseudogene with SVTLE structure, presenting nonsense and frameshift mutations. Our results indicate an association of the lack of thrombin-like activity in B. jararaca and B. erythromelas venoms with mutations and deletions of snake venom thrombin-like enzyme genes. (AU)

FAPESP's process: 19/07618-6 - Hemostasis-inflammation interaction during envenomation by Bothrops jararaca snakes: pathogenesis of thrombocytopenia, and therapeutic anti-ophidian mechanisms of quercetin-3-rutinoside (rutin)
Grantee:Marcelo Larami Santoro
Support Opportunities: Regular Research Grants
FAPESP's process: 15/00003-5 - Snake genes of venom toxins and b-defensins
Grantee:Nancy Oguiura
Support Opportunities: Regular Research Grants