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Toxins 2018, 10(12), 500; https://doi.org/10.3390/toxins10120500

New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom

1
Laboratório de Toxinologia, Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto 14040-903, Brazil
2
Laboratory of Mass Spectrometry, Department of Chemistry, University of Liège, 4000 Liège, Belgium
These authors contributed equally to the conceiving and writing of this manuscript.
*
Authors to whom correspondence should be addressed.
Received: 31 October 2018 / Revised: 22 November 2018 / Accepted: 26 November 2018 / Published: 28 November 2018
(This article belongs to the Section Animal Venoms)
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Abstract

Snake venom serine proteases (SVSPs) are enzymes that are capable of interfering in various parts of the blood coagulation cascade, which makes them interesting candidates for the development of new therapeutic drugs. Herein, we isolated and characterized Moojase, a potent coagulant enzyme from Bothrops moojeni snake venom. The toxin was isolated from the crude venom using a two-step chromatographic procedure. Moojase is a glycoprotein with N-linked glycans, molecular mass of 30.3 kDa and acidic character (pI 5.80–6.88). Sequencing of Moojase indicated that it is an isoform of Batroxobin. Moojase was able to clot platelet-poor plasma and fibrinogen solutions in a dose-dependent manner, indicating thrombin-like properties. Moojase also rapidly induced the proteolysis of the Aα chains of human fibrinogen, followed by the degradation of the Bβ chains after extended periods of incubation, and these effects were inhibited by PMSF, SDS and DTT, but not by benzamidine or EDTA. RP-HPLC analysis of its fibrinogenolysis confirmed the main generation of fibrinopeptide A. Moojase also induced the fibrinolysis of fibrin clots formed in vitro, and the aggregation of washed platelets, as well as significant amidolytic activity on substrates for thrombin, plasma kallikrein, factor Xia, and factor XIIa. Furthermore, thermofluor analyses and the esterase activity of Moojase demonstrated its very high stability at different pH buffers and temperatures. Thus, studies such as this for Moojase should increase knowledge on SVSPs, allowing their bioprospection as valuable prototypes in the development of new drugs, or as biotechnological tools. View Full-Text
Keywords: snake venom; Bothrops moojeni; serine protease; thrombin-like enzyme; coagulation; fibrinogen snake venom; Bothrops moojeni; serine protease; thrombin-like enzyme; coagulation; fibrinogen
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Amorim, F.G.; Menaldo, D.L.; Carone, S.E.I.; Silva, T.A.; Sartim, M.A.; De Pauw, E.; Quinton, L.; Sampaio, S.V. New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom. Toxins 2018, 10, 500.

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