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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 Venomics of Bothrops alternatus is a Pool of Acidic Proteins with Predominant Hemorrhagic and Coagulopathic Activities

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Author(s):
Oehler, Michaela [1] ; Georgieva, Dessislava [2] ; Seifert, Jana [1] ; von Bergen, Martin [1] ; Arni, Raghuvir K. [3] ; Genov, Nicolay [4] ; Betzel, Christian [2]
Total Authors: 7
Affiliation:
[1] UFZ Helmholtz Ctr Environm Res, Helmholtz Ctr Environm Res, Dept Prote, D-04318 Leipzig - Germany
[2] Univ Hamburg, Inst Biochem & Mol Biol, Lab Struct Biol Infect & Inflammat, DESY, D-22603 Hamburg - Germany
[3] UNESP, Dept Phys, IBILCE, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[4] Bulgarian Acad Sci, Inst Organ Chem, BU-1113 Sofia - Bulgaria
Total Affiliations: 4
Document type: Journal article
Source: JOURNAL OF PROTEOME RESEARCH; v. 9, n. 5, p. 2422-2437, MAY 2010.
Web of Science Citations: 43
Abstract

The venom proteome of Bothrops alternatus, a venomous snake widespread in South America, was analyzed by 2-D electrophoresis followed by mass spectrometric analysis and determination of enzymatic activities. The venomic composition revealed that metallo- and serine proteinases play primary roles in the pathogenesis of the envenomation by this pitviper. The identified 100 venom components with molecular masses from 10 to 100 kDa belong to six protein families: metalloproteinases, serine/thrombin-like proteinases, phospholipases A(2), L-amino acid oxidases, disintegrins and thrombin inhibitors. Metalloproteinases predominate and belong exclusively to the P-III class including the most potent hemorrhagic toxins. They represent 50% of all identified proteins. Two isoforms were identified: homologous to jararhagin, a hemorrhagic toxin, and to beritractivase, a nonhemorrhagic and pro-coagulant metalloproteinase. The B. alternatus venom is a rich source of proteins influencing the blood coagulation system with a potential for medical application. The isoelectric points of the components are distributed in the acidic pH range (the p/values are between 4 and 7) and no basic proteins were detected. (AU)