Abstract:
:Triosephosphate isomerase (TPI; EC 5. 3. 1. 1) displayed on the cell surface of Staphylococcus aureus acts as an adhesion molecule that binds to the capsule of Cryptococcus neoformans, a fungal pathogen. This study investigated the function of TPI on the cell surface of S. aureus and its interactions with biological substances such as fibronectin, fibrinogen, plasminogen, and thrombin were investigated. Binding of TPI to plasminogen was demonstrated by both surface plasmon resonance analysis and Far-Western blotting. It is suggested that lysine residues contribute to this binding because the interaction was inhibited by ɛ-aminocaproic acid. Activation of plasminogen to plasmin by staphylokinase or tissue plasminogen activator decreased in the presence of TPI, whereas TPI was degraded by plasmin. In other experiments, intact S. aureus cells had the ability to both increase and decrease plasminogen activation depending on the number of cells. Several molecules expressed on the surface of S. aureus were predicted to interact with plasminogen, resulting in its increased or decreased activation. These findings indicate that S. aureus sometimes localizes and sometimes disseminates in the host, depending on the molecules expressed under various conditions.
journal_name
Microbiol Immunoljournal_title
Microbiology and immunologyauthors
Furuya H,Ikeda Rdoi
10.1111/j.1348-0421.2011.00392.xsubject
Has Abstractpub_date
2011-12-01 00:00:00pages
855-62issue
12eissn
0385-5600issn
1348-0421journal_volume
55pub_type
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