Affiliation:
1. University of Wuerzburg, Institut of Hygiene and Microbiology, Wuerzburg, Germany
2. University of Wuerzburg, Research Center for Infectious Diseases, Wuerzburg, Germany
Abstract
ABSTRACT
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 α
2
-antiplasmin.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
86 articles.
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