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Bacterial killing by heparin-binding peptides from PRELP and thrombospondin

Malmsten, Martin; Davoudi, Mina LU and Schmidtchen, Artur LU (2006) In Matrix Biology 25(5). p.294-300
Abstract
Antimicrobial peptides (AMP) are effector molecules of the innate immune system. A cross-functionality exists between AMPs and heparin-binding peptides. Here, we show that the peptides QPTRRPRPGTGPGRRPRPRPR-P (QPT22), derived from proline arginine-rich end leucine-rich repeat protein (PRELP) and KRFKQDGGWSHWSPWSS (KRF17) from thrombospondin exert antimicrobial activities against the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, as well as against the Gram-positive Bacillus subtilis. Analysis by fluorescence microscopy demonstrated that QPT22 and KRF17 bind to bacterial membranes. Particularly QPT22 was found to induce membrane leakage of liposomes. The peptides displayed no hemolytic activities, nor did they exert... (More)
Antimicrobial peptides (AMP) are effector molecules of the innate immune system. A cross-functionality exists between AMPs and heparin-binding peptides. Here, we show that the peptides QPTRRPRPGTGPGRRPRPRPR-P (QPT22), derived from proline arginine-rich end leucine-rich repeat protein (PRELP) and KRFKQDGGWSHWSPWSS (KRF17) from thrombospondin exert antimicrobial activities against the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, as well as against the Gram-positive Bacillus subtilis. Analysis by fluorescence microscopy demonstrated that QPT22 and KRF17 bind to bacterial membranes. Particularly QPT22 was found to induce membrane leakage of liposomes. The peptides displayed no hemolytic activities, nor did they exert membrane permeabilising effects on human epithelial cells. Additional peptides derived from heparin-binding regions of laminin, vitronectin, and fibronectin exerted similar antibacterial effects. Several peptides also showed activity against Staphylococcus aureus. Thus, the data disclose a novel antimicrobial activity of heparin-binding regions of matrix glycoproteins. The findings can be utilized in the development of novel AMPs for therapeutic use. (c) 2006 Elsevier B.V./Intemational Society of Matrix Biology. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
liposomes, bacteria, heparin, peptide, antimicrobial, membrane
in
Matrix Biology
volume
25
issue
5
pages
294 - 300
publisher
Elsevier
external identifiers
  • pmid:16730966
  • wos:000239028800004
  • scopus:33745475017
ISSN
1569-1802
DOI
10.1016/j.matbio.2006.04.003
language
English
LU publication?
yes
id
b13bc2ed-adb6-4f55-8b05-abd3484bae9a (old id 402120)
date added to LUP
2007-10-09 15:13:13
date last changed
2019-10-02 02:20:58
@article{b13bc2ed-adb6-4f55-8b05-abd3484bae9a,
  abstract     = {Antimicrobial peptides (AMP) are effector molecules of the innate immune system. A cross-functionality exists between AMPs and heparin-binding peptides. Here, we show that the peptides QPTRRPRPGTGPGRRPRPRPR-P (QPT22), derived from proline arginine-rich end leucine-rich repeat protein (PRELP) and KRFKQDGGWSHWSPWSS (KRF17) from thrombospondin exert antimicrobial activities against the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, as well as against the Gram-positive Bacillus subtilis. Analysis by fluorescence microscopy demonstrated that QPT22 and KRF17 bind to bacterial membranes. Particularly QPT22 was found to induce membrane leakage of liposomes. The peptides displayed no hemolytic activities, nor did they exert membrane permeabilising effects on human epithelial cells. Additional peptides derived from heparin-binding regions of laminin, vitronectin, and fibronectin exerted similar antibacterial effects. Several peptides also showed activity against Staphylococcus aureus. Thus, the data disclose a novel antimicrobial activity of heparin-binding regions of matrix glycoproteins. The findings can be utilized in the development of novel AMPs for therapeutic use. (c) 2006 Elsevier B.V./Intemational Society of Matrix Biology. All rights reserved.},
  author       = {Malmsten, Martin and Davoudi, Mina and Schmidtchen, Artur},
  issn         = {1569-1802},
  keyword      = {liposomes,bacteria,heparin,peptide,antimicrobial,membrane},
  language     = {eng},
  number       = {5},
  pages        = {294--300},
  publisher    = {Elsevier},
  series       = {Matrix Biology},
  title        = {Bacterial killing by heparin-binding peptides from PRELP and thrombospondin},
  url          = {http://dx.doi.org/10.1016/j.matbio.2006.04.003},
  volume       = {25},
  year         = {2006},
}