Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria

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

Standard

Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria. / Ehmann, Dirk; Koeninger, Louis; Wendler, Judith; Malek, Nisar P.; Stange, Eduard F.; Wehkamp, Jan; Jensen, Benjamin A.H.

In: Frontiers in Microbiology, Vol. 11, 1147, 2020.

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

Harvard

Ehmann, D, Koeninger, L, Wendler, J, Malek, NP, Stange, EF, Wehkamp, J & Jensen, BAH 2020, 'Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria', Frontiers in Microbiology, vol. 11, 1147. https://doi.org/10.3389/fmicb.2020.01147

APA

Ehmann, D., Koeninger, L., Wendler, J., Malek, N. P., Stange, E. F., Wehkamp, J., & Jensen, B. A. H. (2020). Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria. Frontiers in Microbiology, 11, [1147]. https://doi.org/10.3389/fmicb.2020.01147

Vancouver

Ehmann D, Koeninger L, Wendler J, Malek NP, Stange EF, Wehkamp J et al. Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria. Frontiers in Microbiology. 2020;11. 1147. https://doi.org/10.3389/fmicb.2020.01147

Author

Ehmann, Dirk ; Koeninger, Louis ; Wendler, Judith ; Malek, Nisar P. ; Stange, Eduard F. ; Wehkamp, Jan ; Jensen, Benjamin A.H. / Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria. In: Frontiers in Microbiology. 2020 ; Vol. 11.

Bibtex

@article{56b6b1ff755b4acd8f6d6ca22b46e257,
title = "Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria",
abstract = "The occurrence and spread of multidrug-resistant bacteria is a prominent health concern. To curb this urgent threat, new innovative strategies pursuing novel antimicrobial agents are of the utmost importance. Here, we unleashed the antimicrobial activity of human neutrophil peptide-4 (HNP-4) by tryptic digestion. We identified a single 11 amino acid long fragment (HNP-41–11) with remarkable antimicrobial potential, exceeding that of the full length peptide on both mass and molar levels. Importantly, HNP-41–11 was equally bactericidal against multidrug-resistant and non-resistant strains; a potency that was further enhanced by N- and C-terminus modifications (acetylation and amidation, respectively). These observations, combined with negligible cytotoxicity not exceeding that of the full length peptide, presents proteolytic digestion of innate host-defense-peptides as a novel strategy to overcome the current health crisis related to antibiotic-resistant bacteria.",
keywords = "HNP-4, host defense peptides, multidrug resistance, proteolytic digestion, α-defensins",
author = "Dirk Ehmann and Louis Koeninger and Judith Wendler and Malek, {Nisar P.} and Stange, {Eduard F.} and Jan Wehkamp and Jensen, {Benjamin A.H.}",
year = "2020",
doi = "10.3389/fmicb.2020.01147",
language = "English",
volume = "11",
journal = "Frontiers in Microbiology",
issn = "1664-302X",
publisher = "Frontiers Media S.A.",

}

RIS

TY - JOUR

T1 - Fragmentation of Human Neutrophil α-Defensin 4 to Combat Multidrug Resistant Bacteria

AU - Ehmann, Dirk

AU - Koeninger, Louis

AU - Wendler, Judith

AU - Malek, Nisar P.

AU - Stange, Eduard F.

AU - Wehkamp, Jan

AU - Jensen, Benjamin A.H.

PY - 2020

Y1 - 2020

N2 - The occurrence and spread of multidrug-resistant bacteria is a prominent health concern. To curb this urgent threat, new innovative strategies pursuing novel antimicrobial agents are of the utmost importance. Here, we unleashed the antimicrobial activity of human neutrophil peptide-4 (HNP-4) by tryptic digestion. We identified a single 11 amino acid long fragment (HNP-41–11) with remarkable antimicrobial potential, exceeding that of the full length peptide on both mass and molar levels. Importantly, HNP-41–11 was equally bactericidal against multidrug-resistant and non-resistant strains; a potency that was further enhanced by N- and C-terminus modifications (acetylation and amidation, respectively). These observations, combined with negligible cytotoxicity not exceeding that of the full length peptide, presents proteolytic digestion of innate host-defense-peptides as a novel strategy to overcome the current health crisis related to antibiotic-resistant bacteria.

AB - The occurrence and spread of multidrug-resistant bacteria is a prominent health concern. To curb this urgent threat, new innovative strategies pursuing novel antimicrobial agents are of the utmost importance. Here, we unleashed the antimicrobial activity of human neutrophil peptide-4 (HNP-4) by tryptic digestion. We identified a single 11 amino acid long fragment (HNP-41–11) with remarkable antimicrobial potential, exceeding that of the full length peptide on both mass and molar levels. Importantly, HNP-41–11 was equally bactericidal against multidrug-resistant and non-resistant strains; a potency that was further enhanced by N- and C-terminus modifications (acetylation and amidation, respectively). These observations, combined with negligible cytotoxicity not exceeding that of the full length peptide, presents proteolytic digestion of innate host-defense-peptides as a novel strategy to overcome the current health crisis related to antibiotic-resistant bacteria.

KW - HNP-4

KW - host defense peptides

KW - multidrug resistance

KW - proteolytic digestion

KW - α-defensins

U2 - 10.3389/fmicb.2020.01147

DO - 10.3389/fmicb.2020.01147

M3 - Journal article

C2 - 32582092

AN - SCOPUS:85086587633

VL - 11

JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

SN - 1664-302X

M1 - 1147

ER -

ID: 245616036