Evaluation of the ability of LL-37 to neutralise LPS in vitro and ex vivo

• Published in: PloS one Vol. 6; no. 10; p. e26525
• Main Authors: Scott, Aaron, Weldon, Sinéad, Buchanan, Paul J, Schock, Bettina, Ernst, Robert K, McAuley, Danny F, Tunney, Michael M, Irwin, Chris R, Elborn, J Stuart, Taggart, Clifford C
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 18.10.2011; Public Library of Science (PLoS)
• Subjects: Airway management; Analysis; Anti-Inflammatory Agents - pharmacology; Antibacterial activity; Antimicrobial agents; Antimicrobial Cationic Peptides - pharmacology; Antitoxins - pharmacology; Bacterial infections; Binding; Biology; Bronchitis; Cell Line, Tumor; Cystic fibrosis; Cystic Fibrosis - microbiology; Dentistry; Deoxyribonuclease; Deoxyribonucleic acid; DNA; DNA - metabolism; DNA binding proteins; Drug therapy; Ethics; Flavobacterium; Glycoproteins; Glycosaminoglycans; Glycosaminoglycans - metabolism; Humans; Immune system; Infections; Inflammation; Interleukin 8; Interleukin-8 - biosynthesis; Lipids; Lipopolysaccharides; Lipopolysaccharides - antagonists & inhibitors; Lipopolysaccharides - pharmacology; Lung - microbiology; Lung diseases; Lungs; Mass spectrometry; Medicine; Monocytes; Monocytes - cytology; Monocytes - drug effects; Monocytes - metabolism; Mutagenesis; Mutation; NF-κB protein; Peptides; Pseudomonas aeruginosa; Pseudomonas aeruginosa - chemistry; Scientific imaging; Sepsis; Signal transduction; Signal Transduction - drug effects; Signaling; Sputum; Transcription factors; United Kingdom > UK; Northern Ireland

Human cathelicidin LL-37 is a cationic antimicrobial peptide (AMP) which possesses a variety of activities including the ability to neutralise endotoxin. In this study, we investigated the role of LPS neutralisation in mediating LL-37's ability to inhibit Pseudomonas aeruginosa LPS signalling i...