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Collagen VI Contains Multiple Host Defense Peptides with Potent In Vivo Activity
Lund Univ, Div Infect Med, Dept Clin Sci, Tornavagen 10, S-22184 Lund, Sweden.
Univ Cologne, Fac Med, Ctr Biochem, Ctr Mol Med Cologne, D-50931 Cologne, Germany.
Lund Univ, Div Resp Med & Allergol, Dept Clin Sci, S-22184 Lund, Sweden.
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Farmakognosi.ORCID-id: 0000-0001-9070-6944
Vise andre og tillknytning
2018 (engelsk)Inngår i: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 201, nr 3, s. 1007-1020Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

sted, utgiver, år, opplag, sider
AMER ASSOC IMMUNOLOGISTS , 2018. Vol. 201, nr 3, s. 1007-1020
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-364467DOI: 10.4049/jimmunol.1700602ISI: 000443582200019PubMedID: 29925677OAI: oai:DiVA.org:uu-364467DiVA, id: diva2:1259931
Forskningsfinansiär
Swedish Foundation for Strategic Research , SB12-0019Swedish Research Council, 7480The Crafoord FoundationGerman Research Foundation (DFG), SFB829Tilgjengelig fra: 2018-10-31 Laget: 2018-10-31 Sist oppdatert: 2018-10-31bibliografisk kontrollert

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