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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.)

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

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Amorim, Fernanda G. [1] ; Menaldo, Danilo L. [1] ; Carone, Sante E. I. [1] ; Silva, Thiago A. [1] ; Sartim, Marco A. [1] ; De Pauw, Edwin [2] ; Quinton, Loic [2] ; Sampaio, Suely V. [1]
Total Authors: 8
[1] Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Dept Anal Clin Toxicol & Bromatol, Lab Toxinol, BR-14040903 Ribeirao Preto - Brazil
[2] Univ Liege, Dept Chem, Lab Mass Spectrometry, B-4000 Liege - Belgium
Total Affiliations: 2
Document type: Journal article
Source: TOXINS; v. 10, n. 12 DEC 2018.
Web of Science Citations: 1

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 A chains of human fibrinogen, followed by the degradation of the B 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. (AU)

FAPESP's process: 11/23236-4 - Native and recombinant animal toxins: functional, structural and molecular analysis
Grantee:Suely Vilela
Support type: Research Projects - Thematic Grants
FAPESP's process: 16/20641-9 - Integration of Omics Approaches to Profile the Venom of the Bothrops moojeni snake: unreavelling new toxins and ontogenic divergences
Grantee:Fernanda Gobbi Amorim
Support type: Scholarships abroad - Research Internship - Post-doctor
FAPESP's process: 15/26609-7 - Bothrops moojeni snake venomics: application of toxins of biotechnological interest obtained by omics techniques
Grantee:Fernanda Gobbi Amorim
Support type: Scholarships in Brazil - Post-Doctorate