Production of Mutant Streptokinase Recombinant Protein


Negar Seyed 1 , Parvaneh Shekari 2 , Mojgan Bandehpour 1 , Zarrin Sharifnia 1 , Kazem Parivar 2 , Bahram Kazemi 1 , *

1 Cellular and Molecular Biology Research Center, Shahid Beheshti University, M.C., Tehran, IR Iran

2 Islamic Azad University, Research and Science Campus, Tehran, IR Iran

How to Cite: Seyed N, Shekari P, Bandehpour M, Sharifnia Z, Parivar K, et al. Production of Mutant Streptokinase Recombinant Protein, Arch Clin Infect Dis. Online ahead of Print ; 3(4):179-183.


Archives of Clinical Infectious Diseases: 3 (4); 179-183
Article Type: Research Article


Background: Streptokinase (SK) is most widely used for treatment of myocardial infarction, however, it is the most expensive thrombolytic agent. A major drawback to SK use is the widespread presence of antistreptokinase antibodies (Abs). These Abs cause allergic reactions and neutralize streptokinase therapeutic effects.

Materials and methods: To produce an engineered variant of streptokinase being functional and less antigenic than the native molecule, we cloned and expressed streptokinase mutant gene lacking the C terminal 42 amino acids. Recombinant protein was confirmed by western blot analysis with anti T7 monoclonal antibodies.

Results: pGEMEX-1 expression vector contains T7 gene 10 protein as fusion protein immediately down stream of T7 promoter and before multiple cloning site, streptokinase mutant gene was cloned after fusion protein.

Conclusion: We cloned and expressed mutant streptokinase gene, lacking the C-terminal 42 amino acids. If mut-C42 activity was less affected by neutralizing antibodies compared with native streptokinase, this engineered variant could be a preferred alternative to native streptokinase for thrombolytic therapy.

Full Text

Full text is available in PDF

© 0, Author(s). This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License ( which permits copy and redistribute the material just in noncommercial usages, provided the original work is properly cited.