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A more recent version of this article appeared on October 14, 2005
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M507249200v1
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Papers In Press, published online ahead of print August 9, 2005
J. Biol. Chem, 10.1074/jbc.M507249200
Submitted on July 5, 2005
Revised on August 8, 2005
Accepted on August 9, 2005

Domain 5 of high molecular weight kininogen is antibacterial

Emma Andersson Nordahl, Victoria Rydengård, Matthias Mörgelin, and Artur Schmidtchen

Department of Clinical Sciences, Lund, Section of Dermatology and Venereology, Lund SE-22184

Corresponding Author: emma.nordahl{at}med.lu.se

Antimicrobial peptides are important effectors of the innate immune system. These peptides belong to a multifunctional group of molecules that apart from their antibacterial activities also interact with mammalian cells, glycosaminoglycans, and control chemotaxis, apoptosis, and angiogenesis. Here we demonstrate a novel antimicrobial activity of the heparin-binding and cell-binding domain 5 of high molecular weight kininogen. Antimicrobial epitopes of domain 5 were characterized by analysis of overlapping peptides. A peptide, HKH20 (H479-H498), efficiently killed the Gram-negative bacteria Escherichia coli, Pseudomonas aeruginosa, and the Gram-positive Enterococcus faecalis. Fluorescence microscopy and electron microscopy demonstrated that HKH20 binds to and induces breaks in bacterial membranes. Furthermore, no discernible hemolysis, or membrane permeabilizing effects on eukaryotic cells, were noted. Proteolytic degradation of high molecular weight kininogen by neutrophil-derived proteases as well as the metalloproteinase elastase from Pseudomonas aeruginosa yielded fragments comprising HKH20 epitopes, indicating that kininogen-derived antibacterial peptides are released during proteolysis.


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