Activating the Cpx response induces tolerance to antisense PNA delivered by an arginine-rich peptide in Escherichia coli

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Activating the Cpx response induces tolerance to antisense PNA delivered by an arginine-rich peptide in Escherichia coli. / Frimodt-Møller, Jakob; Koulouktsis, Andreas; Charbon, Godefroid; Otterlei, Marit; Nielsen, Peter E.; Løbner-Olesen, Anders.

In: Molecular Therapy - Nucleic Acids, Vol. 25, 2021, p. 444-454.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Frimodt-Møller, J, Koulouktsis, A, Charbon, G, Otterlei, M, Nielsen, PE & Løbner-Olesen, A 2021, 'Activating the Cpx response induces tolerance to antisense PNA delivered by an arginine-rich peptide in Escherichia coli', Molecular Therapy - Nucleic Acids, vol. 25, pp. 444-454. https://doi.org/10.1016/j.omtn.2021.06.009

APA

Frimodt-Møller, J., Koulouktsis, A., Charbon, G., Otterlei, M., Nielsen, P. E., & Løbner-Olesen, A. (2021). Activating the Cpx response induces tolerance to antisense PNA delivered by an arginine-rich peptide in Escherichia coli. Molecular Therapy - Nucleic Acids, 25, 444-454. https://doi.org/10.1016/j.omtn.2021.06.009

Vancouver

Frimodt-Møller J, Koulouktsis A, Charbon G, Otterlei M, Nielsen PE, Løbner-Olesen A. Activating the Cpx response induces tolerance to antisense PNA delivered by an arginine-rich peptide in Escherichia coli. Molecular Therapy - Nucleic Acids. 2021;25:444-454. https://doi.org/10.1016/j.omtn.2021.06.009

Author

Frimodt-Møller, Jakob ; Koulouktsis, Andreas ; Charbon, Godefroid ; Otterlei, Marit ; Nielsen, Peter E. ; Løbner-Olesen, Anders. / Activating the Cpx response induces tolerance to antisense PNA delivered by an arginine-rich peptide in Escherichia coli. In: Molecular Therapy - Nucleic Acids. 2021 ; Vol. 25. pp. 444-454.

Bibtex

@article{aafb17227385405bb49f5dc7598e01d4,
title = "Activating the Cpx response induces tolerance to antisense PNA delivered by an arginine-rich peptide in Escherichia coli",
abstract = "Cell-penetrating peptides (CPPs) are increasingly used for cellular drug delivery in both pro- and eukaryotic cells, and oligoarginines have attracted special attention. How arginine-rich CPPs translocate across the cell envelope, particularly for prokaryotes, is still unknown. Arginine-rich CPPs efficiently deliver antimicrobial peptide nucleic acid (PNA) to its intracellular mRNA target in bacteria. We show that resistance to PNA conjugated to an arginine-rich CPP in Escherichia coli requires multiple genetic modifications and is specific for the CPP part and not to the PNA part. An integral part of the resistance was the constitutively activated Cpx-envelope stress response system (cpx∗), which decreased the cytoplasmic membrane potential. This indicates an indirect energy-dependent uptake mechanism for antimicrobials conjugated to arginine-rich CPPs. In agreement, cpx∗ mutants showed low-level resistance to aminoglycosides and an arginine-rich CPP conjugated to a peptide targeting the DNA sliding clamp, i.e., similar uptake in E. coli for these antimicrobial compounds.",
author = "Jakob Frimodt-M{\o}ller and Andreas Koulouktsis and Godefroid Charbon and Marit Otterlei and Nielsen, {Peter E.} and Anders L{\o}bner-Olesen",
note = "{\textcopyright} 2021 The Author(s).",
year = "2021",
doi = "10.1016/j.omtn.2021.06.009",
language = "English",
volume = "25",
pages = "444--454",
journal = "Molecular Therapy - Nucleic Acids",
issn = "2162-2531",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Activating the Cpx response induces tolerance to antisense PNA delivered by an arginine-rich peptide in Escherichia coli

AU - Frimodt-Møller, Jakob

AU - Koulouktsis, Andreas

AU - Charbon, Godefroid

AU - Otterlei, Marit

AU - Nielsen, Peter E.

AU - Løbner-Olesen, Anders

N1 - © 2021 The Author(s).

PY - 2021

Y1 - 2021

N2 - Cell-penetrating peptides (CPPs) are increasingly used for cellular drug delivery in both pro- and eukaryotic cells, and oligoarginines have attracted special attention. How arginine-rich CPPs translocate across the cell envelope, particularly for prokaryotes, is still unknown. Arginine-rich CPPs efficiently deliver antimicrobial peptide nucleic acid (PNA) to its intracellular mRNA target in bacteria. We show that resistance to PNA conjugated to an arginine-rich CPP in Escherichia coli requires multiple genetic modifications and is specific for the CPP part and not to the PNA part. An integral part of the resistance was the constitutively activated Cpx-envelope stress response system (cpx∗), which decreased the cytoplasmic membrane potential. This indicates an indirect energy-dependent uptake mechanism for antimicrobials conjugated to arginine-rich CPPs. In agreement, cpx∗ mutants showed low-level resistance to aminoglycosides and an arginine-rich CPP conjugated to a peptide targeting the DNA sliding clamp, i.e., similar uptake in E. coli for these antimicrobial compounds.

AB - Cell-penetrating peptides (CPPs) are increasingly used for cellular drug delivery in both pro- and eukaryotic cells, and oligoarginines have attracted special attention. How arginine-rich CPPs translocate across the cell envelope, particularly for prokaryotes, is still unknown. Arginine-rich CPPs efficiently deliver antimicrobial peptide nucleic acid (PNA) to its intracellular mRNA target in bacteria. We show that resistance to PNA conjugated to an arginine-rich CPP in Escherichia coli requires multiple genetic modifications and is specific for the CPP part and not to the PNA part. An integral part of the resistance was the constitutively activated Cpx-envelope stress response system (cpx∗), which decreased the cytoplasmic membrane potential. This indicates an indirect energy-dependent uptake mechanism for antimicrobials conjugated to arginine-rich CPPs. In agreement, cpx∗ mutants showed low-level resistance to aminoglycosides and an arginine-rich CPP conjugated to a peptide targeting the DNA sliding clamp, i.e., similar uptake in E. coli for these antimicrobial compounds.

U2 - 10.1016/j.omtn.2021.06.009

DO - 10.1016/j.omtn.2021.06.009

M3 - Journal article

C2 - 34484867

VL - 25

SP - 444

EP - 454

JO - Molecular Therapy - Nucleic Acids

JF - Molecular Therapy - Nucleic Acids

SN - 2162-2531

ER -

ID: 279186165