Expression and partial biochemical characterization of a recombinant serine protease from Bothrops pauloensis snake venom

Snake venom serine proteases (SVSPs) are enzymes capable of interfering at several points of hemostasis. Some serine proteases present thrombin-like activity, which makes them targets for the development of therapeutics agents in the treatment of many hemostatic disorders. In this study, a recombina...

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Bibliographic Details
Published in:	Toxicon (Oxford) Vol. 115; pp. 49 - 54
Main Authors:	Isabel, Thais F., Costa, Guilherme Nunes Moreira, Pacheco, Isabela B., Barbosa, Luana G., Santos-Junior, Célio D., Fonseca, Fernando P.P., Boldrini França, Johara, Henrique-Silva, Flávio, Yoneyama, Kelly A.G., Rodrigues, Renata S., Rodrigues, Veridiana de Melo
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 01-06-2016
Subjects:	Amino Acid Sequence Animals Biochemistry Blood Coagulation - drug effects Bothrops Bothrops pauloensis Cattle Chemical compounds Disorders Enzymes Fibrinogen - chemistry Hemostatic Disorders - drug therapy Hemostatics Heterologous expression Hydrolysis - drug effects Pharmacology Protease Recombinant Recombinant Proteins - chemistry serine protease Serine Proteases - chemistry Snake venom Snake Venoms - enzymology Thrombin - chemistry Thrombin-like Snake venom Bothrops pauloensis serine protease Thrombin-like Heterologous expression
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Summary:	Snake venom serine proteases (SVSPs) are enzymes capable of interfering at several points of hemostasis. Some serine proteases present thrombin-like activity, which makes them targets for the development of therapeutics agents in the treatment of many hemostatic disorders. In this study, a recombinant thrombin-like serine protease, denominated rBpSP-II, was obtained from cDNA of the Bothrops pauloensis venom gland and was characterized enzymatically and biochemically. The enzyme rBpSP-II showed clotting activity on bovine plasma and proteolytic activity on fibrinogen, cleaving exclusively the Aα chain. The evaluation of rBpSP-II activity on chromogenic substrates demonstrated thrombin-like activity of the enzyme due to its capacity to hydrolyze the thrombin substrate. These characteristics make rBpSP-II an attractive molecule for additional studies. Further research is needed to verify whether rBpSP-II can serve as a template for the synthesis of therapeutic agents to treat hemostatic disorders. •rBpSP-II showed sequence identity ranging from 83% to 96% to other snake venom serine proteases.•rBpSP-II showed activity on chromogenic substrates demonstrated thrombin-like activity.•rBpSP-II can serve as template for synthesis of therapeutic agents to treat hemostatic disorders.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0041-0101 1879-3150
DOI:	10.1016/j.toxicon.2016.03.002