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Cationic bactericidal peptide 1018 does not specifically target the stringent response alarmone (p)ppGpp
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS). University of Tartu, Institute of Technology, Nooruse 1, 50411 Tartu, Estonia.
2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, 36549Article in journal (Refereed) Published
Abstract [en]

The bacterial stringent response is a key regulator of bacterial virulence, biofilm formation and antibiotic tolerance, and is a promising target for the development of new antibacterial compounds. The intracellular nucleotide (p)ppGpp acts as a messenger orchestrating the stringent response. A synthetic peptide 1018 was recently proposed to specifically disrupt biofilms by inhibiting the stringent response via direct interaction with (p) ppGpp (de la Fuente-Nunez et al. (2014) PLoS Pathogens). We have interrogated the specificity of the proposed molecular mechanism. When inhibition of Pseudomonas aeruginosa planktonic and biofilm growth is tested simultaneously in the same assay, peptides 1018 and the control peptide 8101 generated by an inversion of the amino acid sequence of 1018 are equally potent, and, importantly, do not display a preferential activity against biofilm. 1018 inhibits planktonic growth of Escherichia coli equally efficiently either when the alleged target, (p) ppGpp, is essential (MOPS media lacking amino acid L-valine), or dispensable for growth (MOPS media supplemented with L-valine). Genetic disruption of the genes relA and spoT responsible for (p) ppGpp synthesis moderately sensitizes-rather than protects-E. coli to 1018. We suggest that the antimicrobial activity of 1018 does not rely on specific recognition of the stringent response messenger (p) ppGpp.

Place, publisher, year, edition, pages
2016. Vol. 6, 36549
National Category
Biochemistry and Molecular Biology Microbiology in the medical area
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URN: urn:nbn:se:umu:diva-129841DOI: 10.1038/srep36549ISI: 000387043700001PubMedID: 27819280OAI: oai:DiVA.org:umu-129841DiVA: diva2:1065099
Available from: 2017-01-13 Created: 2017-01-09 Last updated: 2017-01-13Bibliographically approved

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Andresen, LiisHauryliuk, Vasili
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CiteExportLink to record
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Citation style
  • apa
  • harvard1
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  • vancouver
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  • de-DE
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