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  • 1.
    Abdillahi, Suado M.
    et al.
    Lund Univ, Div Infect Med, Dept Clin Sci, Tornavagen 10, S-22184 Lund, Sweden.
    Maass, Tobias
    Univ Cologne, Fac Med, Ctr Biochem, Ctr Mol Med Cologne, D-50931 Cologne, Germany.
    Kasetty, Gopinath
    Lund Univ, Div Resp Med & Allergol, Dept Clin Sci, S-22184 Lund, Sweden.
    Strömstedt, Adam A.
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Farmakognosi.
    Baumgarten, Maria
    Lund Univ, Div Infect Med, Dept Clin Sci, Tornavagen 10, S-22184 Lund, Sweden.
    Tati, Ramesh
    Lund Univ, Div Infect Med, Dept Clin Sci, Tornavagen 10, S-22184 Lund, Sweden.
    Nordin, Sara L.
    Lund Univ, Div Infect Med, Dept Clin Sci, Tornavagen 10, S-22184 Lund, Sweden.
    Walse, Björn
    Sarom Biostruct AB, S-22363 Lund, Sweden.
    Wagener, Raimund
    Univ Cologne, Fac Med, Ctr Biochem, Ctr Mol Med Cologne, D-50931 Cologne, Germany.
    Schmidtchen, Artur
    Lund Univ, Div Dermatol & Venereol, Dept Clin Sci, S-22184 Lund, Sweden;Univ Copenhagen, Bispebjerg Hosp, Dept Biomed Sci, Copenhagen Wound Healing Ctr, DK-2400 Copenhagen, Denmark.
    Mörgelin, Matthias
    Lund Univ, Div Infect Med, Dept Clin Sci, Tornavagen 10, S-22184 Lund, Sweden;Colzyx AB, S-22381 Lund, Sweden.
    Collagen VI Contains Multiple Host Defense Peptides with Potent In Vivo Activity2018Inngår i: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 201, nr 3, s. 1007-1020Artikkel i tidsskrift (Fagfellevurdert)
    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.

  • 2.
    Saravanan, Rathi
    et al.
    Nanyang Technol Univ, Lee Kong Chian Sch Med, 59 Nanyang Dr, Singapore 636921, Singapore.
    Holdbrook, Daniel A.
    ASTAR, Bioinformat Inst, 30 Biopolis St,07-01 Matrix, Singapore 138671, Singapore.
    Petrlova, Jitka
    Lund Univ, Dept Clin Sci, Div Dermatol & Venereol, SE-22184 Lund, Sweden.
    Singh, Shalini
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för farmaci.
    Berglund, Nils A.
    ASTAR, Bioinformat Inst, 30 Biopolis St,07-01 Matrix, Singapore 138671, Singapore;Aarhus Univ, Dept Chem, Langelandsgade 140, DK-8000 Aarhus C, Denmark.
    Choong, Yeu Khai
    Nanyang Technol Univ, Lee Kong Chian Sch Med, 59 Nanyang Dr, Singapore 636921, Singapore.
    Kjellstrom, Sven
    Lund Univ, Biomed Ctr D13, CEBMMS, Lund, Sweden.
    Bond, Peter J.
    Natl Univ Singapore, Dept Biol Sci, 14 Sci Dr, Singapore 117543, Singapore;ASTAR, Bioinformat Inst, 30 Biopolis St,07-01 Matrix, Singapore 138671, Singapore.
    Malmsten, Martin
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för farmaci. Univ Copenhagen, Dept Pharm, DK-2100 Copenhagen, Denmark.
    Schmidtchen, Artur
    Univ Copenhagen, Dept Biomed Sci, Bispebjerg Hosp, Copenhagen Wound Healing Ctr, DK-2400 Copenhagen, Denmark;Lund Univ, Dept Clin Sci, Div Dermatol & Venereol, SE-22184 Lund, Sweden;Nanyang Technol Univ, Lee Kong Chian Sch Med, 59 Nanyang Dr, Singapore 636921, Singapore.
    Structural basis for endotoxin neutralisation and anti-inflammatory activity of thrombin-derived C-terminal peptides2018Inngår i: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 9, artikkel-id 2762Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Thrombin-derived C-terminal peptides (TCPs) of about 2 kDa are present in wounds, where they exert anti-endotoxic functions. Employing a combination of nuclear magnetic resonance spectroscopy (NMR), biophysical, mass spectrometry and cellular studies combined with in silico multiscale modelling, we here determine the bound conformation of HVF18 (HVFRLKKWIQKVIDQFGE), a TCP generated by neutrophil elastase, in complex with bacterial lipopolysaccharide (LPS) and define a previously undisclosed interaction between TCPs and human CD14. Further, we show that TCPs bind to the LPS-binding hydrophobic pocket of CD14 and identify the peptide region crucial for TCP interaction with LPS and CD14. Taken together, our results demonstrate the role of structural transitions in LPS complex formation and CD14 interaction, providing a molecular explanation for the previously observed therapeutic effects of TCPs in experimental models of bacterial sepsis and endotoxin shock.

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