Interaction of cationic antimicrobial peptides with Mycoplasma pulmonis. Issue 20 (28th August 2013)

• Record Type: Journal Article
• Authors: Park, Ho Jin; Kang, Ki Mo; Dybvig, Kevin; Lee, Bok Luel; Jung, Yong Woo; Lee, In Hee
• Is Part Of: FEBS letters. Volume 587:Issue 20(2013)
• Page Start: 3321
• Page End: 3326
• Publication Date: 2013-08-28
• Subjects: AMP -- antimicrobial peptide -- POPC -- 1-palmytoyl-2-oleoyl l-α-phosphatidylcholine -- POPG -- 1-palmytoyl-2-oleoyl l-α-phosphatidylglycerol -- CL -- cardiolipin -- SPM -- sphingomyelin -- NaP -- sodium phosphate -- PI -- propidium iodine -- SEM -- scanning electron microscopy -- TLC -- two-dimensional thin layer chromatography -- EPS -- exopolysaccharide -- Vsa -- variable surface antigen -- Antimicrobial peptide -- Mycoplasma -- Phospholipid -- Liposome -- Action mechanism; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.08.016
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : We investigated the mode of action underlying the anti‐mycoplasma activity of cationic antimicrobial peptides (AMPs) using four known AMPs and Mycoplasma pulmonis as a model mycoplasma. Scanning electron microscopy revealed that the integrity of the M. pulmonis membrane was significantly damaged within 30 min of AMPs exposure, which was confirmed by measuring the uptake of propidium iodine into the mycoplasma cells. The anti‐mycoplasma activity of AMPs was found to depend on the binding affinity for phosphatidylcholine, which was incorporated into the mycoplasma membrane from the growth medium and preferentially distributed in the outer leaflet of the lipid bilayer. Abstract : We examine the action mechanism of antimicrobial peptides against mycoplasma. The mechanism relies on interaction of antimicrobial peptides with membrane lipids. Binding to phosphatidylcholine is critical for their anti‐mycoplasma activity.