title: Antibacterial and anti-biofilm effects of cathelicidin peptides against pathogens isolated from cystic fibrosis patients.
abstract: Six different cathelicidin-derived peptides were compared to tobramycin for antibacterial and anti-biofilm effects against S. aureus, P. aeruginosa, and S. maltophilia strains isolated from cystic fibrosis patients. Overall, SMAP-29, BMAP-28, and BMAP-27 showed relevant antibacterial activity (MIC(50) 4-8μg/ml), and in some cases higher than tobramycin. In contrast, indolicidin, LL-37, and Bac7(1-35) showed no significant antimicrobial activity (MIC(50)>32μg/ml). Killing kinetics experiments showed that in contrast to tobramycin the active cathelicidin peptides exert a rapid bactericidal activity regardless of the species tested. All three peptides significantly reduced biofilm formation by S. maltophilia and P. aeruginosa strains at 1/2× MIC, although at a lower extent than tobramycin. In addition, BMAP-28, as well as tobramycin, was also active against S. aureus biofilm formation. Preformed biofilms were significantly affected by bactericidal SMAP-29, BMAP-27 and BMAP-28 concentrations, although at a lesser extent than tobramycin. Overall, our results indicate the potential of some cathelicidin-derived peptides for the development of novel therapeutic agents for cystic fibrosis lung disease.
authors.affiliation: Department of Biomedical Sciences, G. d'Annunzio University of Chieti-Pescara, Via Vestini 31, 66100 Chieti, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Pompilio
authors.forename: M
authors.initials: M
authors.lastname: Scocchi
authors.forename: S
authors.initials: S
authors.lastname: Pomponio
authors.forename: F
authors.initials: F
authors.lastname: Guida
authors.forename: A
authors.initials: A
authors.lastname: Di Primio
authors.forename: E
authors.initials: E
authors.lastname: Fiscarelli
authors.forename: R
authors.initials: R
authors.lastname: Gennaro
authors.forename: G
authors.initials: G
authors.lastname: Di Bonaventura
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology; D018441:Biofilms / Q000187:drug effects*; D001798:Blood Proteins / Q000494:pharmacology; D054804:Cathelicidins / Q000494:pharmacology*; D002417:Cattle; D003550:Cystic Fibrosis / Q000382:microbiology*; D016905:Gram-Negative Bacterial Infections / Q000382:microbiology; D006801:Humans; D008826:Microbial Sensitivity Tests; D008855:Microscopy, Electron, Scanning; D008969:Molecular Sequence Data; D011506:Proteins / Q000494:pharmacology; D011550:Pseudomonas aeruginosa / Q000187:drug effects / Q000302:isolation & purification / Q000648:ultrastructure; D012756:Sheep; D013203:Staphylococcal Infections / Q000382:microbiology; D013211:Staphylococcus aureus / Q000187:drug effects / Q000302:isolation & purification; D020615:Stenotrophomonas maltophilia / Q000187:drug effects / Q000302:isolation & purification; D014031:Tobramycin / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; C102359:BMAP-27; C102360:BMAP-28; C481640:Bac7(1-35) peptide; D001798:Blood Proteins; D054804:Cathelicidins; D011506:Proteins; C403305:SMAP29 protein, Ovis aries; C073143:indolicidin; D014031:Tobramycin