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Investigation into the mechanism of action of the antimicrobial peptides Os and Os-C derived from a tick defensin

•Os and Os-C caused altered intracellular morphology of E. coli and B. subtilis.•Membrane effects were observed with fluorescence and TEM studies.•Os and Os-C were able to enter bacterial cells.•The peptides may have intracellular targets such as DNA.•Differences observed between Os and Os-C indicat...

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Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2015-09, Vol.71, p.179-187
Main Authors: Taute, Helena, Bester, Megan J., Neitz, Albert W.H., Gaspar, Anabella R.M.
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container_title Peptides (New York, N.Y. : 1980)
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description •Os and Os-C caused altered intracellular morphology of E. coli and B. subtilis.•Membrane effects were observed with fluorescence and TEM studies.•Os and Os-C were able to enter bacterial cells.•The peptides may have intracellular targets such as DNA.•Differences observed between Os and Os-C indicate dissimilar modes of action. Os and Os-C are two novel antimicrobial peptides, derived from a tick defensin, which have been shown to have a larger range of antimicrobial activity than the parent peptide, OsDef2. The aim of this study was to determine whether the peptides Os and Os-C are mainly membrane acting, or if these peptides have possible additional intracellular targets in Escherichia coli and Bacillus subtilis. Transmission electron microscopy revealed that both peptides adversely affected intracellular structure of both bacteria causing different degrees of granulation of the intracellular contents. At the minimum bactericidal concentrations, permeabilization as determined with the SYTOX green assay seemed not to be the principle mode of killing when compared to melittin. However, fluorescent triple staining indicated that the peptides caused permeabilization of stationary phase bacteria and TEM indicated membrane effects. Studies using fluorescently labeled peptides revealed that the membrane penetrating activity of Os and Os-C was similar to buforin II. Os-C was found to associate with the septa of B. subtilis. Plasmid binding studies showed that Os and Os-C binds E. coli plasmid DNA at a similar charge ratio as melittin. These studies suggest membrane activity for Os and Os-C with possible intracellular targets such as DNA. The differences in permeabilization at lower concentrations and binding to DNA between Os and Os-C, suggest that the two peptides have dissimilar modes of action.
doi_str_mv 10.1016/j.peptides.2015.07.017
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issn 0196-9781
1873-5169
language eng
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subjects Animals
Argasidae - chemistry
Arthropod Proteins - chemistry
Arthropod Proteins - pharmacology
Bacillus subtilis - growth & development
Bacillus subtilis - ultrastructure
C-terminus
Defensin
Defensins - chemistry
Defensins - pharmacology
DNA binding
Escherichia coli - growth & development
Escherichia coli - ultrastructure
Membrane permeabilization
Mode of action
Tick
title Investigation into the mechanism of action of the antimicrobial peptides Os and Os-C derived from a tick defensin
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