dc.contributor.author |
Taute, Helena
|
|
dc.contributor.author |
Bester, Megan Jean
|
|
dc.contributor.author |
Neitz, Albert Walter Herman
|
|
dc.contributor.author |
Gaspar, Anabella Regina Marques
|
|
dc.date.accessioned |
2015-10-30T07:30:10Z |
|
dc.date.issued |
2015-09 |
|
dc.description.abstract |
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. |
en_ZA |
dc.description.embargo |
2016-09-30 |
|
dc.description.librarian |
hb2015 |
en_ZA |
dc.description.sponsorship |
Medical Research Council and the National Research Foundation of South Africa. |
en_ZA |
dc.description.uri |
http://www.elsevier.com/locate/peptides |
en_ZA |
dc.identifier.citation |
Taute, H, Bester, MJ, Neitz, AWH & Gaspar, ARM 2015, 'Investigation into the mechanism of action of the antimicrobial peptides Os and Os-C derived from a tick defensin', Peptides, vol. 71, pp. 179-187. |
en_ZA |
dc.identifier.issn |
0196-9781 (print) |
|
dc.identifier.issn |
1873-5169 (online) |
|
dc.identifier.other |
10.1016/j.peptides.2015.07.017 |
|
dc.identifier.uri |
http://hdl.handle.net/2263/50276 |
|
dc.language.iso |
en |
en_ZA |
dc.publisher |
Elsevier |
en_ZA |
dc.rights |
© 2015 Elsevier Inc. All rights reserved. Notice : this is the author’s version of a work that was accepted for publication in Peptides. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Peptides, vol. 71, pp. 179-187, 2015. doi : 10.1016/j.peptides.2015.07.017. |
en_ZA |
dc.subject |
Defensin |
en_ZA |
dc.subject |
Tick |
en_ZA |
dc.subject |
C-terminus |
en_ZA |
dc.subject |
Membrane permeabilization |
en_ZA |
dc.subject |
Mode of action |
en_ZA |
dc.subject |
DNA binding |
en_ZA |
dc.subject.other |
Health sciences article SDG-03 |
|
dc.subject.other |
SDG-03: Good health and well-being |
|
dc.subject.other |
Health sciences article SDG-17 |
|
dc.subject.other |
SDG-17: Partnerships for the goals |
|
dc.title |
Investigation into the mechanism of action of the antimicrobial peptides Os and Os-C derived from a tick defensin |
en_ZA |
dc.type |
Postprint Article |
en_ZA |