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Staphylokinase is a 16 kDa profibrinolytic protein produced by certain strains of *Staphylococcus aureus*. It acts as a plasminogen activator, inducing highly fibrin-specific thrombolysis by converting plasminogen to plasmin in the presence of fibrin. This mechanism enables it to dissolve blood clots with high selectivity for fibrin, reducing the risk of systemic bleeding compared to other thrombolytics. Recombinant forms have been developed with reduced immunogenicity and enhanced activity. Clinical trials—including phase 3 studies—have demonstrated that non-immunogenic recombinant staphylokinase (e.g., Fortelyzin) is non-inferior to alteplase for acute ischemic stroke and may offer advantages such as single bolus administration and lower production costs[1][4][5]. Staphylokinase also interacts with host immune peptides (such as α-defensins), which can modulate both its antimicrobial and thrombolytic activities[6][8].
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