Binding of plasminogen to Escherichia coli adhesion proteins.

Abstract

Immobilization of plasminogen via its lysine-binding sites is regarded as a prerequisite for its activation and function in fibrinolysis and pericellular proteolysis. In the present study, the interaction of plasminogen with fimbriae found on Escherichia coli strains causing invasive human infections was studied. Plasminogen displayed concentration-dependent and saturable binding to immobilized type 1 fimbriae and, several fold lower binding to P and S fimbriae. The binding to fimbriae was effectively inhibited by epsilon-aminocaproic acid indicating that it was mediated by the lysine-binding sites of plasminogen. Binding studies with mutated fimbriae and inhibition tests indicated that the interaction was not dependent on the lectin subunit of the fimbriae. These results indicate the existence of a novel type of host-microbe interaction which may be important in the invasion by bacteria of host tissues.

• Authors: J Parkkinen, T K Korhonen
• Journal: FEBS letters (FEBS Lett) Vol. 250 Issue 2 Pg. 437-40 (Jul 03 1989) ISSN: 0014-5793 [Print] England
• PMID: 2568948 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Adhesins, Escherichia coli
• Bacterial Outer Membrane Proteins
• Plasminogen
• Aminocaproic Acid

Topics

• Adhesins, Escherichia coli
• Aminocaproic Acid (pharmacology)
• Bacterial Adhesion
• Bacterial Outer Membrane Proteins (metabolism)
• Escherichia coli (metabolism)
• Fimbriae, Bacterial (metabolism)
• Plasminogen (metabolism)