[21] Streptokinase

Castellino, Francis J.; Sodetz, James M.; Brockway, William J.; Siefring, Gerald E.

doi:10.1016/s0076-6879(76)45024-3

Cited by 93 publications

(47 citation statements)

References 20 publications

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“…The majority of GAS strains that cause human diseases secrete a plasminogen activator, streptokinase (Ska). The latter forms a 1:1 stoichiometric complex with plasminogen, converts other plasminogen molecules into active plasmin, and is not regulated by host fluid phase ␣ 2 -antiplasmin (Apl) (10).…”

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confidence: 99%

Role of the C-Terminal Lysine Residues of Streptococcal Surface Enolase in Glu- and Lys-Plasminogen-Binding Activities of Group A Streptococci

et al. 2004

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Streptococcal surface enolase (SEN) is a major plasminogen-binding protein of group A streptococci. Our earlier biochemical studies have suggested that the region responsible for this property is likely located at the C-terminal end of the SEN molecule. In the present study, the gene encoding SEN was cloned from group A streptococci M6 isolate D471. A series of mutations in the sen gene corresponding to the C-terminal region ( 428 KSFYNLKK 435 ) of the SEN molecule were created by either deleting one or more terminal lysine residues or replacing them with leucine. All purified recombinant SEN proteins with altered C-terminal ends were found to be enzymatically active and were analyzed for their Glu-and Lys-plasminogen-binding activities. Wild-type SEN bound to Lys-plasminogen with almost three times more affinity than to Glu-plasminogen. However, the recombinant mutant SEN proteins with a deletion of Lys434-435 or with K435L and K434-435L replacements showed a significant decrease in Glu-and Lys-plasminogen-binding activities. Accordingly, a streptococcal mutant expressing SEN-K434-435L showed a significant decrease in Glu-and Lys-plasminogen-binding activities. Biochemical and functional analyses of the isogenic mutant strain revealed a significant decrease in its abilities to cleave a chromogenic tripeptide substrate, acquire plasminogen from human plasma, and penetrate the extracellular matrix. Together, these data indicate that the last two C-terminal lysine residues of surfaceexposed SEN contribute significantly to the plasminogen-binding activity of intact group A streptococci and hence to their ability to exploit host properties to their own advantage in tissue invasion.

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Role of the C-Terminal Lysine Residues of Streptococcal Surface Enolase in Glu- and Lys-Plasminogen-Binding Activities of Group A Streptococci

et al. 2004

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“…Notably, these bacterial activators can modify the specificity of the bound host proteinase toward macromolecular substrates by providing novel docking sites for substrate recognition (8). The mechanism of nonproteolytic, cofactor-induced activation has been intensively investigated for streptokinase (SK), a Pg activator secreted by ␤-hemolytic streptococci (9,10), as well as for staphylocoagulase (SC), a prothrombin (ProT) activator from Staphylococcus aureus (11)(12)(13). Another Pg activator from S. aureus, staphylokinase, is structurally related to SK (8,14) but requires active plasmin (Pm) to form an activator complex of free Pg molecules (15,16).…”

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Structural Basis for Reduced Staphylocoagulase-mediated Bovine Prothrombin Activation

Friedrich

Panizzi

Kawabata

et al. 2006

Journal of Biological Chemistry

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“…Streptokinase (STK), a protein of 415 amino acids that does not contain disulfide bridges, is produced and excreted by some strains of ß-hemolytic streptococci (1,2). Because of its ability to activate the fibrinolytic system, it is currently used as a thrombolytic agent for the treatment of patients with acute myocardial infarction (3,4).…”

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confidence: 99%

Cloning, expression and purification of recombinant streptokinase: partial characterization of the protein expressed in Escherichia coli

Avilán¹,

Yarzábal²,

Jurgensen³

et al. 1997

Braz J Med Biol Res

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We cloned the streptokinase (STK) gene of Streptococcus equisimilis in an expression vector of Escherichia coli to overexpress the profibrinolytic protein under the control of a tac promoter. Almost all the recombinant STK was exported to the periplasmic space and recovered after gentle lysozyme digestion of induced cells. The periplasmic fraction was chromatographed on DEAE Sepharose followed by chromatography on phenyl-agarose. Active proteins eluted between 4.5 and 0% ammonium sulfate, when a linear gradient was applied. Three major STK derivatives of 47.5 kDa, 45 kDa and 32 kDa were detected by Western blot analysis with a polyclonal antibody. The 32-kDa protein formed a complex with human plasminogen but did not exhibit Glu-plasminogen activator activity, as revealed by a zymographic assay, whereas the 45-kDa protein showed a K m = 0.70 µM and k cat = 0.82 s -1 , when assayed with a chromogen-coupled substrate. These results suggest that these proteins are putative fragments of STK, possibly derived from partial degradation during the export pathway or the purification steps. The 47.5-kDa band corresponded to the native STK, as revealed by peptide sequencing.

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[21] Streptokinase

Cited by 93 publications

References 20 publications

Role of the C-Terminal Lysine Residues of Streptococcal Surface Enolase in Glu- and Lys-Plasminogen-Binding Activities of Group A Streptococci

Role of the C-Terminal Lysine Residues of Streptococcal Surface Enolase in Glu- and Lys-Plasminogen-Binding Activities of Group A Streptococci

Structural Basis for Reduced Staphylocoagulase-mediated Bovine Prothrombin Activation

Cloning, expression and purification of recombinant streptokinase: partial characterization of the protein expressed in Escherichia coli

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