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Domain 5 of high molecular weight kininogen is antibacterial.

Nordahl, Emma LU ; Rydengård, Victoria LU ; Mörgelin, Matthias LU and Schmidtchen, Artur LU (2005) In Journal of Biological Chemistry 280(41). p.34832-34839
Abstract
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 and 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 (His(479) - His(498)), efficiently killed the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa and the Gram-positive Enterococcus faecalis. Fluorescence microscopy and electron microscopy... (More)
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 and 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 (His(479) - His(498)), efficiently killed the Gram-negative bacteria Escherichia coli and 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 P. aeruginosa yielded fragments comprising HKH20 epitopes, indicating that kininogen-derived antibacterial peptides are released during proteolysis. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
280
issue
41
pages
34832 - 34839
publisher
ASBMB
external identifiers
  • wos:000232403900055
  • scopus:27144555794
ISSN
1083-351X
DOI
10.1074/jbc.M507249200
language
English
LU publication?
yes
id
0103b8c3-7d89-4ca1-b3e8-60680369e46e (old id 142873)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16091369&dopt=Abstract
date added to LUP
2007-07-11 16:14:04
date last changed
2017-09-10 03:46:40
@article{0103b8c3-7d89-4ca1-b3e8-60680369e46e,
  abstract     = {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 and 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 (His(479) - His(498)), efficiently killed the Gram-negative bacteria Escherichia coli and 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 P. aeruginosa yielded fragments comprising HKH20 epitopes, indicating that kininogen-derived antibacterial peptides are released during proteolysis.},
  author       = {Nordahl, Emma and Rydengård, Victoria and Mörgelin, Matthias and Schmidtchen, Artur},
  issn         = {1083-351X},
  language     = {eng},
  number       = {41},
  pages        = {34832--34839},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Domain 5 of high molecular weight kininogen is antibacterial.},
  url          = {http://dx.doi.org/10.1074/jbc.M507249200},
  volume       = {280},
  year         = {2005},
}