Plasminogen interaction and activation on Streptococcus mutans surface

L. Urdaneta, G. Vanegas, G. Premoli, L. Avilan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

A number of pathogenic microorganisms have been previously shown to bind plasminogen. The subsequent activation of plasminogen into plasmin can contribute to their virulence. In this study, we have shown that Streptococcus mutans is able to bind both human plasminogen and plasmin. Binding of plasminogen to S. mutans was inhibited by L-lysine and epsilon-aminocaproic acid, indicating that binding is mediated via lysine-binding sites of plasminogen. S. mutans enhanced the activation of plasminogen by tissue plasminogen activator but not by urokinase. This enhancement turned out to be dependent on cell concentration. Zymogram analysis showed that the plasmin activity acquired after plasminogen binding and activation is the most important proteolytic activity in the strain tested. These results suggest a mechanism involving acquisition of a host protease that might contribute to the infective process of this microorganism.

Original languageEnglish
Pages (from-to)257-261
Number of pages5
JournalOral Microbiology and Immunology
Volume19
Issue number4
Early online date22 Jun 2004
DOIs
Publication statusPublished - Aug 2004

Keywords

  • Aminocaproates/pharmacology
  • Binding Sites
  • Fibrinolysin/metabolism
  • Humans
  • In Vitro Techniques
  • Lysine/pharmacology
  • Plasminogen/metabolism
  • Protein Binding/drug effects
  • Streptococcus mutans/genetics
  • Virulence

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