Bacteria may cope differently from similar membrane damage caused by the Australian tree frog antimicrobial peptide maculatin 1.1

Sani, Marc-Antoine, Henriques, Sonia Troeira, Weber, Daniel and Separovic, Frances (2015) Bacteria may cope differently from similar membrane damage caused by the Australian tree frog antimicrobial peptide maculatin 1.1. Journal of Biological Chemistry, 290 32: 19853-19862. doi:10.1074/jbc.M115.643262

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Author Sani, Marc-Antoine
Henriques, Sonia Troeira
Weber, Daniel
Separovic, Frances
Title Bacteria may cope differently from similar membrane damage caused by the Australian tree frog antimicrobial peptide maculatin 1.1
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 1083-351X
0021-9258
Publication date 2015-08-07
Sub-type Article (original research)
DOI 10.1074/jbc.M115.643262
Open Access Status File (Publisher version)
Volume 290
Issue 32
Start page 19853
End page 19862
Total pages 10
Place of publication Rockville, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2016
Language eng
Formatted abstract
Maculatin 1.1 (Mac1) is an antimicrobial peptide from the skin of Australian tree frogs and is known to possess selectivity toward Gram-positive bacteria. Although Mac1 has membrane disrupting activity, it is not known how Mac1 selectively targets Gram-positive over Gram-negative bacteria. The interaction of Mac1 with Escherichia coli, Staphylococcus aureus, and human red blood cells (hRBC) and with their mimetic model membranes is here reported. The peptide showed a 16-fold greater growth inhibition activity against S. aureus (4 μM) than against E. coli (64 μM) and an intermediate cytotoxicity against hRBC (30 μM). Surprisingly, Sytox Green uptake monitored by flow cytometry showed that Mac1 compromised both bacterial membranes with similar efficiency at ∼20-fold lower concentration than the reported minimum inhibition concentration against S. aureus. Mac1 also reduced the negative potential of S. aureus and E. coli membrane with similar efficacy. Furthermore, liposomes mimicking the cell membrane of S. aureus (POPG/TOCL) and E. coli (POPE/POPG) were lysed at similar concentrations, whereas hRBC-like vesicles (POPC/SM/Chol) remained mostly intact in the presence of Mac1. Remarkably, when POPG/TOCL and POPE/POPG liposomes were co-incubated, Mac1 did not induce leakage from POPE/POPG liposomes, suggesting a preference toward POPG/TOCL membranes that was supported by surface plasma resonance assays. Interestingly, circular dichroism spectroscopy showed a similar helical conformation in the presence of the anionic liposomes but not the hRBC mimics. Overall, the study showed that Mac1 disrupts bacterial membranes in a similar fashion before cell death events and would preferentially target S. aureus over E. coli or hRBC membranes.
Keyword Bacteria
Membrane damage
Australian tree frog antimicrobial peptide maculatin
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
Institute for Molecular Bioscience - Publications
 
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