Domain 5 of high molecular weight kininogen is antibacterial.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/142873
- author
- Nordahl, Emma LU ; Rydengård, Victoria LU ; Mörgelin, Matthias LU and Schmidtchen, Artur LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 280
- issue
- 41
- pages
- 34832 - 34839
- publisher
- American Society for Biochemistry and Molecular Biology
- 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
- 2016-04-01 12:21:37
- date last changed
- 2022-03-28 23:51:39
@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 = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Domain 5 of high molecular weight kininogen is antibacterial.}},
url = {{https://lup.lub.lu.se/search/files/2891413/624929.pdf}},
doi = {{10.1074/jbc.M507249200}},
volume = {{280}},
year = {{2005}},
}