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Infection and Immunity, April 2004, p. 2416-2419, Vol. 72, No. 4
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.4.2416-2419.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus pneumoniae Is a Surface-Displayed Plasminogen-Binding Protein

Simone Bergmann,1 Manfred Rohde,2 and Sven Hammerschmidt1*

Research Center for Infectious Diseases, University of Würzburg, Würzburg,1 GBF-German Research Centre for Biotechnology, Braunschweig, Germany2

Received 18 August 2003/ Returned for modification 7 November 2003/ Accepted 22 December 2003

The recruitment of plasminogen endows the bacterial cell surface of Streptococcus pneumoniae with proteolytic activity. In this study we demonstrate specific plasmin- and plasminogen-binding activity for the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is located in the cytoplasm as well as on the surface of pneumococci. GAPDH exhibits a high affinity for plasmin and a significantly lower affinity for plasminogen.

* Corresponding author. Mailing address: Research Center for Infectious Diseases, University of Würzburg, Röntgenring 11, 97070 Würzburg, Germany. Phone: 0049-931-312153. Fax: 0049-931-312578 E-mail: s.hammerschmidt{at}mail.uni-wuerzburg.de.

Editor: V. J. DiRita

Infection and Immunity, April 2004, p. 2416-2419, Vol. 72, No. 4
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.4.2416-2419.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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