Collagen VI contains multiple host defense peptides with potent in vivo activity
(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.
(Less)
- author
- organization
- publishing date
- 2018-08-01
- type
- 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
- pmid:29925677
- 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
- 2024-09-18 00:35:49
@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}}, doi = {{10.4049/jimmunol.1700602}}, volume = {{201}}, year = {{2018}}, }