Antimicrobial activities of LL-37 and its truncated variants against Burkholderia thailandensis.
Antimicrobial peptides (AMPs) are essential host defence molecules found in a wide variety of species and are promising antibacterial therapeutic candidates. Focusing on the human cathelicidin peptide LL-37, the aim of the present study was to explore the mechanisms of action and antimicrobial activities of a library of LL-37 fragments using Burkholderia thailandensis E264 as a model. The results revealed that IG-19 was the shortest fragment within LL-37 that exhibited antibacterial activity. LL-31, missing six residues at the C-terminus of LL-37, exhibited the strongest killing effect. Freeze-fracture electron microscopy of bacterial cells treated with either LL-37 or LL-31 revealed irregular bacterial surfaces with bleb projections, indicating that these peptides disrupted the integrity of the membrane. In addition, these peptides induced leakage of cell components, including nucleotides and even proteins. Altogether, the results obtained indicate the potential of using LL-31 as a new AMP to combat Burkholderia spp.
Kanthawong
Sakawarat
S
Department of Microbiology, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand.
Bolscher
Jan G M
JG
Veerman
Enno C I
EC
van Marle
Jan
J
Nazmi
Kamran
K
Wongratanacheewin
Surasakdi
S
Taweechaisupapong
Suwimol
S
D023181:Antimicrobial Cationic Peptides / Q000235:genetics / Q000494:pharmacology*; D019117:Burkholderia / Q000187:drug effects* / Q000648:ultrastructure; D002462:Cell Membrane / Q000187:drug effects / Q000648:ultrastructure; D006801:Humans; D050296:Microbial Viability / Q000187:drug effects; D046529:Microscopy, Electron, Transmission; D050505:Mutant Proteins / Q000494:pharmacology*; D017384:Sequence Deletion; D013329:Structure-Activity Relationship; D054804:Cathelicidins
D023181:Antimicrobial Cationic Peptides; D050505:Mutant Proteins; D054804:Cathelicidins