Antimicrobial activity of trout hepcidin

Álvarez, Claudio; Guzmán, Fanny; Cárdenas, Constanza; Marshall, Sergio H.; Mercado, Luís

doi:10.1016/j.fsi.2014.04.013

Cited by 82 publications

(60 citation statements)

References 45 publications

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“…The antimicrobial activities of hepcidins from many fish species have been demonstrated, includinghepcidins from tilapia [6e12], turbot [13,14], black porgy [15], medaka [16], orange-spotted grouper [17], rare minnow [18], gilthead seabream [19], trout [20], large yellow croaker [21], zebrafish [22], channel catfish [23], Japanese flounder [24], half-smooth tongue sole [25], and sea bass [26]. Hepcidins used in antimicrobial analyses have generally been synthetic or recombinant peptides, which have consistently demonstrated antibacterial activity against Gram-positive and Gram-negative bacteria.…”

Section: Introductionmentioning

confidence: 99%

Two hepcidins from spotted scat (Scatophagus argus) possess antibacterial and antiviral functions in vitro

Liu

Zhang

et al. 2016

Fish & Shellfish Immunology

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Section: Introductionmentioning

confidence: 99%

Two hepcidins from spotted scat (Scatophagus argus) possess antibacterial and antiviral functions in vitro

Liu

Zhang

et al. 2016

Fish & Shellfish Immunology

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“…In addition, it was shown that the antimicrobial activity of human Hep-25 was enhanced in presence of copper [8]. A recent study on trout hepcidin-25 showed similar results [9]. Melino et al have demonstrated that the same Nterminal region is responsible for the metal binding capacity of hepcidin-25.…”

Section: Introductionmentioning

confidence: 83%

“…In studies for the structural analysis of Hep-25 using NMR spectroscopy and molecular dynamics simulations [11,24], the presence of the copper ions was largely ignored. Interestingly, a 3D model of the copper complex of trout hepcidin-25 was proposed [9], yet based on the outdated structural template [12].…”

Section: Analysis Of Hepcidin-metal Complexesmentioning

confidence: 99%

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Investigations of the Copper Peptide Hepcidin-25 by LC-MS/MS and NMR

Abbas

Vranić

Hoffmann

et al. 2018

Preprint

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Abstract:Hepcidin-25 was identified as the main iron regulator in the human body by binding to the sole ironexporter ferroportin. Studies showed that the N-terminus of hepcidin is responsible for this interaction, the same N-terminus that encompasses a small copper(II)-binding site known as ATCUN (amino terminal Cu(II)-and Ni(II)-binding) motif. Interestingly, this copper-binding property is largely ignored in most papers dealing with hepcidin-25. In this context, detailed investigations of the formed complex of hepcidin-25 with copper could reveal insights into its biological role. The present work is mainly focused on the study of the metal-bound form of hepcidin-25, which could be considered the biologically active form. The first part is devoted to the reversed-phase chromatographic separation of copper-bound and copper-free hepcidin-25, which was achieved by applying basic mobile phases containing 0.1% ammonia. Further, mass spectrometry (tandem mass spectrometry MS/MS, high resolution mass spectrometry HRMS) and nuclear magnetic resonance (NMR) spectroscopy were employed to characterize the copper-peptide. Lastly, a 3D model of hepcidin-25 with bound copper(II) is presented. The identification of metal complexes and potential isoforms and isomers, from which the latter usually are left undetected by mass spectrometry, led to the conclusion that complementary analytical methods are needed to characterize a peptide calibrant or reference material comprehensively. Quantitative nuclear magnetic resonance (qNMR), inductively-coupled plasma mass spectrometry (ICP-MS), ion-mobility spectrometry (IMS) and chiral amino acid analysis (AAA) should be considered among others.

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“…As a defense antimicrobial peptide, hepcidins from mammals, amphibians, and fish have been shown to exhibit antimicrobial effects against various Gram-negative and Gram-positive bacteria (Alvarez et al 2014;Krause et al 2000). As a result, hepcidin is considered an important component of the innate immune defense system.…”

Section: Introductionmentioning

confidence: 99%

Porcine Hepcidin Exerts an Iron-Independent Bacteriostatic Activity Against Pathogenic Bacteria

Liú

Xiong

et al. 2014

Int J Pept Res Ther

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Hepcidin was first identified as an antimicrobial peptide and later demonstrated that hepcidin is the long sought hormone to regulate iron homeostasis in mammals. Though its iron regulatory function has been extensively investigated, the studies on its antimicrobial properties are limited. The aim of current study was to evaluate the antibacterial activity of synthetic porcine hepcidin (pHepc) in vitro against pathogen bacteria via radial diffusion, colony forming count, transmission electron microscopy and DNA binding assays. Our results showed that pHepc exerted little bactericidal activity, but possessed bacteriostatic activity by reducing the viable Escherichia coli K88, E. coli ATCC 25922, Staphylococcus aureus ATCC 25923 and Salmonella typhimurium CMCC 50013. pHepc-treated E. coli K88 exhibited longer cells and cytoplasm unevenly distribution, while pHepc-treated S. aureus led to cytoplasm leakage and partly lysis of bacterial cells. Gel retardation assay showed the existence of the binding affinity of pHepc for DNA. In addition, pHepc retained the bacteriostatic activity in a wide range of pH value from 4.0 to 8.0 or in the presence of iron, respectively. Considering the high expression in response to infection and the bacteriostatic activity, pHepc may be an important defense molecule for pig health.

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Antimicrobial activity of trout hepcidin

Cited by 82 publications

References 45 publications

Two hepcidins from spotted scat (Scatophagus argus) possess antibacterial and antiviral functions in vitro

Two hepcidins from spotted scat (Scatophagus argus) possess antibacterial and antiviral functions in vitro

Investigations of the Copper Peptide Hepcidin-25 by LC-MS/MS and NMR

Porcine Hepcidin Exerts an Iron-Independent Bacteriostatic Activity Against Pathogenic Bacteria

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