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Enhanced activation of bound plasminogen on Staphylococcus aureus by staphylokinase
Author(s) -
Mölkänen Tomi,
Tyynelä Jaana,
Helin Jari,
Kalkkinen Nisse,
Kuusela Pentti
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02580-2
Subject(s) - staphylokinase , staphylococcus aureus , chemistry , microbiology and biotechnology , biology , bacteria , genetics
Activation of plasminogen (plg) to plasmin by the staphylococcal activator, staphylokinase (SAK), is effectively regulated by the circulating inhibitor, α 2 ‐antiplasmin (α 2 AP). 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 α 2 AP 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.