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http://purl.uniprot.org/citations/18443119http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18443119http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18443119http://www.w3.org/2000/01/rdf-schema#comment"Granulocyte chemotactic protein 2 (GCP-2)/CXCL6 is a CXC chemokine expressed by macrophages and epithelial and mesenchymal cells during inflammation. Through binding and activation of its receptors (CXCR1 and CXCR2), it exerts neutrophil-activating and angiogenic activities. Here we show that GCP-2/CXCL6 itself is antibacterial. Antibacterial activity against gram-positive and gram-negative pathogenic bacteria of relevance to mucosal infections was seen at submicromolar concentrations (minimal bactericidal concentration at which 50% of strains tested were killed, 0.063 +/- 0.01 to 0.37 +/-0.03 muM). In killed bacteria, GCP-2/CXCL6 associated with bacterial surfaces, which showed membrane disruption and leakage. A structural prediction indicated the presence of three antiparallel NH(2)-terminal beta-sheets and a short amphipathic COOH-terminal alpha-helix; the latter feature is typical of antimicrobial peptides. However, when the synthetic derivatives corresponding to the NH(2)-terminal (50 amino acids) and COOH-terminal (19 amino acids, corresponding to the putative alpha-helix) regions were compared, higher antibacterial activity was observed for the NH(2)-terminus-derived peptide, indicating that the holopeptide is necessary for full antibacterial activity. An artificial model of bacterial membranes confirmed these findings. The helical content of GCP-2/CXCL6 in the presence or absence of lipopolysaccharide or negatively charged membranes was studied by circular dichroism. As with many antibacterial peptides, membrane disruption by GCP-2/CXCL6 was dose-dependently reduced in the presence of NaCl, which, we here demonstrate, inhibited the binding of the peptide to the bacterial surface. Compared with CXC chemokines ENA-78/CXCL5 and NAP-2/CXCL7, GCP-2/CXCL6 showed a 90-fold-higher antibacterial activity. Taken together, GCP/CXCL6, in addition to its chemotactic and angiogenic properties, is likely to contribute to direct antibacterial activity during localized infection."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.org/dc/terms/identifier"doi:10.1128/aac.00028-08"xsd:string
http://purl.uniprot.org/citations/18443119http://purl.org/dc/terms/identifier"doi:10.1128/aac.00028-08"xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Morgelin M."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Morgelin M."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Collin M."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Collin M."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Malmsten M."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Malmsten M."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Egesten A."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Egesten A."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Linge H.M."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Linge H.M."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Nordenfelt P."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/author"Nordenfelt P."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/name"Antimicrob. Agents Chemother."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/name"Antimicrob. Agents Chemother."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/pages"2599-2607"xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/pages"2599-2607"xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/title"The human CXC chemokine granulocyte chemotactic protein 2 (GCP-2)/CXCL6 possesses membrane-disrupting properties and is antibacterial."xsd:string
http://purl.uniprot.org/citations/18443119http://purl.uniprot.org/core/title"The human CXC chemokine granulocyte chemotactic protein 2 (GCP-2)/CXCL6 possesses membrane-disrupting properties and is antibacterial."xsd:string
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