Enhanced activation of bound plasminogen on Staphylococcus aureus by staphylokinase

FEBS Letters

Tyynelä, Jaana²  Mölkänen, Tomi³  Helin, Jari¹  Kalkkinen, Nisse¹  Kuusela, Pentti³ 

[1] Laboratory of Protein Chemistry, Institute of Biotechnology, University of Helsinki, Helsinki, Finland;Protein Chemistry Unit and Institute of Biomedicine, Biomedicum, Helsinki, Finland;Department of Bacteriology and Immunology, The Haartman Institute, P.O. Box 21 (Haartmaninkatu 3), FIN-00014 University of Helsinki, Helsinki, Finland

关键词: Plasminogen;    Staphylokinase;    Activation of plasminogen;    Staphylococcus aureus;   

DOI  :  10.1016/S0014-5793(02)02580-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Activation of plasminogen (plg) to plasmin by the staphylococcal activator, staphylokinase (SAK), is effectively regulated by the circulating inhibitor, α₂-antiplasmin (α₂AP). 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 α₂AP 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, α-enolase, and ribonucleotide reductase subunit 2, respectively.

【 授权许可】

Unknown