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Thromb Haemost 2005; 94(02): 304-311
DOI: 10.1160/TH05-05-0369
Theme Issue Article
Schattauer GmbH

The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration

Simone Bergmann
1   Research Center for Infectious Diseases, University of Würzburg, Würzburg
,
Manfred Rohde
2   GBF-German Research Centre for Biotechnology, Braunschweig
,
Klaus T. Preissner
3   Institute for Biochemistry, Justus-Liebig-University, Giessen, Germany
,
Sven Hammerschmidt
1   Research Center for Infectious Diseases, University of Würzburg, Würzburg
› Author AffiliationsGrant support: This work was supported in part by the Deutsche Forschungsgemeinschaft to S. Hammerschmidt (Sonderforschungsbereich Grant 479-A7), M. Rohde (DFG-Ro 2407/1), and the Bundesministerium für Bildung und Forschung to S. Hammerschmidt (BMBF-CAPNETZ C8).
Further Information

Publication History

Received: 27 May 2005

Accepted after major revision: 01 July 2005

Publication Date:
05 December 2017 (online)

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Summary

The glycolytic enzyme α-enolase represnts one of the nonclassical cell surface plasminogen-binding proteins of Streptococcus pneumoniae. In this study we investigated the impact of an internal plasminogen-binding motif of enolase on degradation of extracellular matrix and pneumococcal transmigration. In the presence of host-derived plasminogen activators (PA) tissuetype PA or urokinase PA and plasminogen S. pneumoniae expressing wild-type enolase efficiently degraded Matrigel or extracellular matrix (ECM). In contrast, amino acid substitutions in the nine residue plasminogen-binding motif of enolase significantly reduced degradation of ECM or Matrigel by mutated pneumococci. Similarly, recombinant wild-type enolase but not a mutated enolase derivative that lacks plasminogen-binding activity efficiently degraded ECM and Matrigel, respectively. In particular, bacterial cell enolase-bound plasmin potentiated dissolution of fibrin or laminin and transmigration of pneumococci through a fibrin matrix. In conclusion, these results provide evidence that the enolase is the major plasminogen-binding protein of pneumococci and that the nine residue plasminogen-binding motif of enolase is the key cofactor for plasmin-mediated pneumococcal degradation and transmigration through host ECM.

Keywords

Pneumococci - plasmin activity - enolase - fibrinolysis - degradation
 

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