Streptokinase is a potent plasminogen activator widely used as a thrombolytic agent in clinical settings. It is naturally secreted by several strains of beta-hemolytic streptococci, particularly Streptococcus equisimilis . Streptokinase works by converting plasminogen to plasmin, which then breaks down fibrin clots, making it an essential treatment for conditions such as myocardial infarction, pulmonary embolism, and deep vein thrombosis .
The natural production of streptokinase has several limitations, including low yields and the pathogenic nature of its native host. To overcome these challenges, recombinant DNA technology has been employed to produce streptokinase in various host organisms. One notable example is the expression of streptokinase in the Gram-positive bacterium Streptomyces lividans .
In this process, the structural gene encoding streptokinase is fused to signal sequences that facilitate its secretion. For instance, the Streptomyces venezuelae CBS762.70 subtilisin inhibitor (vsi) signal sequence or the Streptomyces lividans xylanase C (xlnC) signal sequence can be used . The recombinant production in Streptomyces lividans has shown higher yields when the Sec-dependent signal peptide mediates the translocation of streptokinase .
Recombinant streptokinase offers several advantages over its naturally produced counterpart:
Streptokinase is primarily used as a thrombolytic agent to dissolve blood clots in patients suffering from acute myocardial infarction, pulmonary embolism, and other thrombotic conditions . Its ability to activate plasminogen and subsequently degrade fibrin clots makes it a critical component in emergency medicine.