Format:
Online-Ressource
ISSN:
1469-3178
Content:
Abstract: The bacterial toxin CcdB (Controller of Cell death or division B) targets DNA Gyrase, an essential bacterial topoisomerase, which is also the molecular target for fluoroquinolones. Here, we present a short cell‐penetrating 24‐mer peptide, CP1‐WT, derived from the Gyrase‐binding region of CcdB and examine its effect on growth of Escherichia coli, Salmonella Typhimurium, Staphylococcus aureus and a carbapenem‐ and tigecycline‐resistant strain of Acinetobacter baumannii in both axenic cultures and mouse models of infection. The CP1‐WT peptide shows significant improvement over ciprofloxacin in terms of its in vivo therapeutic efficacy in treating established infections of S. Typhimurium, S. aureus and A. baumannii. The molecular mechanism likely involves inhibition of Gyrase or Topoisomerase IV, depending on the strain used. The study validates the CcdB binding site on bacterial DNA Gyrase as a viable and alternative target to the fluoroquinolone binding site.
In:
day:11
In:
month:05
In:
year:2023
In:
extent:30
In:
European Molecular Biology Organization, EMBO reports, Heidelberg : EMBO Press, [200]-, (11.05.2023) (gesamt 30), 1469-3178
Language:
English
DOI:
10.15252/embr.202255338
URN:
urn:nbn:de:101:1-2023051115361276094863
URL:
https://doi.org/10.15252/embr.202255338
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023051115361276094863
URL:
https://d-nb.info/1289105774/34
URL:
https://doi.org/10.15252/embr.202255338
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