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Journal of Bacteriology, April 2007, p. 3246-3255, Vol. 189, No. 8
0021-9193/07/$08.00+0 doi:10.1128/JB.01966-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Martin V. R. Weber,1,
Sven Hammerschmidt,2
Simone Bergmann,2
Matthias Frosch,1 and
Oliver Kurzai1
University of Wuerzburg, Institut of Hygiene and Microbiology, Wuerzburg, Germany,1 University of Wuerzburg, Research Center for Infectious Diseases, Wuerzburg, Germany2
Received 29 December 2006/ Accepted 6 February 2007
Plasminogen recruitment is a common strategy of pathogenic bacteria and results in a broad-spectrum surface-associated protease activity. Neisseria meningitidis has previously been shown to bind plasminogen. In this study, we show by several complementary approaches that endolase, DnaK, and peroxiredoxin, which are usually intracellular proteins, can also be located in the outer membrane and act as plasminogen receptors. Internal binding motifs, rather than C-terminal lysine residues, are responsible for plasminogen binding of the N. meningitidis receptors. Recombinant receptor proteins inhibit plasminogen association with N. meningitidis in a concentration-dependent manner. Besides binding purified plasminogen, N. meningitidis can also acquire plasminogen from human serum. Activation of N. meningitidis-associated plasminogen by urokinase results in functional activity and allows the bacteria to degrade fibrinogen. Furthermore, plasmin bound to N. meningitidis is protected against inactivation by
2-antiplasmin.
Published ahead of print on 16 February 2007.
A.K and M.V.R.W. contributed equally to this study.
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