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FEBS Lett. 2002 Apr 24;517(1-3):72-8.

Enhanced activation of bound plasminogen on Staphylococcus aureus by staphylokinase.

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Department of Bacteriology and Immunology, The Haartman Institute, FIN-00014 University of Helsinki, Helsinki, Finland.


Activation of plasminogen (plg) to plasmin by the staphylococcal activator, staphylokinase (SAK), is effectively regulated by the circulating inhibitor, alpha2-antiplasmin (alpha2AP). Here it is demonstrated that intact Staphylococcus aureus cells and solubilized staphylococcal cell wall proteins not only protected SAK-promoted plg activation against the inhibitory effect of alpha2AP but also enhanced the activation. The findings suggest that the surface-associated plg activation by SAK may have an important physiological function in helping staphylococci in tissue dissemination. Amino acid sequencing of tryptic peptides originating from the 59-, 56- and 43-kDa proteins, isolated as putative plg-binding proteins, identified them as staphylococcal inosine 5'-monophosphate dehydrogenase, alpha-enolase, and ribonucleotide reductase subunit 2, respectively.

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