Recombinant production of <Emphasis Type="Italic">Streptococcus equisimilis</Emphasis> streptokinase by <Emphasis Type="Italic">Streptomyces lividans</Emphasis> |
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Authors: | Elsa Pimienta Julio C Ayala Caridad Rodríguez Astrid Ramos Lieve Van Mellaert Carlos Vallín Jozef Anné |
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Institution: | 1.Departamento de Investigaciones Biomédicas,Laboratorio de Genética, Centro de Química Farmacéutica,Ciudad de la Habana,Cuba;2.Laboratory of Bacteriology, Rega Institute, Katholieke Universiteit Leuven,Leuven,Belgium |
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Abstract: | Background Streptokinase (SK) is a potent plasminogen activator with widespread clinical use as a thrombolytic agent. It is naturally
secreted by several strains of beta-haemolytic streptococci. The low yields obtained in SK production, lack of developed gene
transfer methodology and the pathogenesis of its natural host have been the principal reasons to search for a recombinant
source for this important therapeutic protein. We report here the expression and secretion of SK by the Gram-positive bacterium
Streptomyces lividans. The structural gene encoding SK was fused to the Streptomyces venezuelae CBS762.70 subtilisin inhibitor (vsi) signal sequence or to the Streptomyces lividans xylanase C (xlnC) signal sequence. The native Vsi protein is translocated via the Sec pathway while the native XlnC protein uses the twin-arginine
translocation (Tat) pathway. |
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