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Cytosolic Proteins Contribute to Surface Plasminogen Recruitment of Neisseria meningitidis

Andreas Knaust,^1*, 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.