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Collagen VI contains multiple host defense peptides with potent in vivo activity

Abdillahi, Suado M. LU ; Maaß, Tobias; Kasetty, Gopinath LU ; Strömstedt, Adam A.; Baumgarten, Maria LU ; Tati, Ramesh LU ; Nordin, Sara L. LU ; Walse, Björn LU ; Wagener, Raimund and Schmidtchen, Artur LU , et al. (2018) In Journal of Immunology 201(3). p.1007-1020
Abstract

Collagen VI is a ubiquitous extracellular matrix component that forms extensive microfibrillar networks in most connective tissues. In this study, we describe for the first time, to our knowledge, that the collagen VI von Willebrand factor type A-like domains exhibit a broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria in human skin infections in vivo. In silico sequence and structural analysis of VWA domains revealed that they contain cationic and amphipathic peptide sequence motifs, which might explain the antimicrobial nature of collagen VI. In vitro and in vivo studies show that these peptides exhibited significant antibacterial activity against Staphylococcus aureus, Escherichia coli, and... (More)

Collagen VI is a ubiquitous extracellular matrix component that forms extensive microfibrillar networks in most connective tissues. In this study, we describe for the first time, to our knowledge, that the collagen VI von Willebrand factor type A-like domains exhibit a broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria in human skin infections in vivo. In silico sequence and structural analysis of VWA domains revealed that they contain cationic and amphipathic peptide sequence motifs, which might explain the antimicrobial nature of collagen VI. In vitro and in vivo studies show that these peptides exhibited significant antibacterial activity against Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa through membrane disruption. Our findings shed new light on the role of collagen VI-derived peptides in innate host defense and provide templates for development of peptide-based antibacterial therapies.

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Contribution to journal
publication status
published
subject
in
Journal of Immunology
volume
201
issue
3
pages
14 pages
publisher
American Association of Immunologists
external identifiers
  • scopus:85050759000
ISSN
0022-1767
DOI
10.4049/jimmunol.1700602
language
English
LU publication?
yes
id
3fecd06b-19c2-4676-b21c-8f88b7ab9fce
date added to LUP
2018-08-22 12:16:53
date last changed
2019-02-20 11:24:40
@article{3fecd06b-19c2-4676-b21c-8f88b7ab9fce,
  abstract     = {<p>Collagen VI is a ubiquitous extracellular matrix component that forms extensive microfibrillar networks in most connective tissues. In this study, we describe for the first time, to our knowledge, that the collagen VI von Willebrand factor type A-like domains exhibit a broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria in human skin infections in vivo. In silico sequence and structural analysis of VWA domains revealed that they contain cationic and amphipathic peptide sequence motifs, which might explain the antimicrobial nature of collagen VI. In vitro and in vivo studies show that these peptides exhibited significant antibacterial activity against Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa through membrane disruption. Our findings shed new light on the role of collagen VI-derived peptides in innate host defense and provide templates for development of peptide-based antibacterial therapies.</p>},
  author       = {Abdillahi, Suado M. and Maaß, Tobias and Kasetty, Gopinath and Strömstedt, Adam A. and Baumgarten, Maria and Tati, Ramesh and Nordin, Sara L. and Walse, Björn and Wagener, Raimund and Schmidtchen, Artur and Mörgelin, Matthias},
  issn         = {0022-1767},
  language     = {eng},
  month        = {08},
  number       = {3},
  pages        = {1007--1020},
  publisher    = {American Association of Immunologists},
  series       = {Journal of Immunology},
  title        = {Collagen VI contains multiple host defense peptides with potent in vivo activity},
  url          = {http://dx.doi.org/10.4049/jimmunol.1700602},
  volume       = {201},
  year         = {2018},
}