Importance of the disulfide bridges in the antibacterial activity of human hepcidin

Hocquellet, Agnès; Sénéchal, Caroline Le; Garbay, Bertrand

doi:10.1016/j.peptides.2012.06.001

Cited by 57 publications

(33 citation statements)

References 27 publications

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“…With human Hepc25, the lack of SYTOX uptake showed that membrane permeabilization does not occur [173] in contrast to most antimicrobial peptides [150]. Similar results have been observed with fish peptides, using light emission kinetics, which showed that Medaka recombinant pro-hepcidin and synthetic hepcidin also do not cause membrane permeabilization in E. coli [171].…”

Section: Hepcidinsmentioning

confidence: 72%

Antimicrobial Peptides from Fish

2014

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Antimicrobial peptides (AMPs) are found widely distributed through Nature, and participate in the innate host defense of each species. Fish are a great source of these peptides, as they express all of the major classes of AMPs, including defensins, cathelicidins, hepcidins, histone-derived peptides, and a fish-specific class of the cecropin family, called piscidins. As with other species, the fish peptides exhibit broad-spectrum antimicrobial activity, killing both fish and human pathogens. They are also immunomodulatory, and their genes are highly responsive to microbes and innate immuno-stimulatory molecules. Recent research has demonstrated that some of the unique properties of fish peptides, including their ability to act even in very high salt concentrations, make them good potential targets for development as therapeutic antimicrobials. Further, the stimulation of their gene expression by exogenous factors could be useful in preventing pathogenic microbes in aquaculture.

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Section: Hepcidinsmentioning

confidence: 72%

Antimicrobial Peptides from Fish

2014

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“…This response could retard extracellular bacterial growth, as iron is essential for replication (60). Moreover, the direct anti-bacterial activity of human hepcidin (61) (13,(21)(22)(23). These regions could be involved in the binding and labile release of hepcidin and demonstrate that an equilibrium is set up between protein-bound and free hepcidin that could explain urinary hepcidin excretion (2).…”

Section: Discussionmentioning

confidence: 99%

Hepcidin Bound to α2-Macroglobulin Reduces Ferroportin-1 Expression and Enhances Its Activity at Reducing Serum Iron Levels

Huang

Austin

Sari

et al. 2013

Journal of Biological Chemistry

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Background:Hepcidin is the hormone of iron metabolism that is bound by ␣ 2 -macroglobulin (␣ 2 M) and its activated counterpart (␣ 2 M-MA). Results: Serum iron is reduced to a greater extent in mice treated with ␣ 2 M⅐hepcidin or ␣ 2 M-MA⅐hepcidin relative to unbound hepcidin. Conclusion: ␣ 2 M retards hepcidin excretion by the kidney, increasing its efficacy. Significance: These results are important for understanding hepcidin transport and detection in blood.

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“…It has antimicrobial activity against several bacteria, such as A. hydrophila, E. coli, Vibrio prahaemoloyticus, S. aureus, Micrococcus luteus, and Bacillus subtilis [14]. It has been demonstrated that the disulfide bridges were essential for antibacterial activity of human hepcidin [38]. However, two types of trout hepcidin (reduced and oxidized) all could inhibit the growth of E. coli and Piscirickettsia salmonis, and the oxidized peptide is more effective than the one reduced [4].…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)

Fei

Wang

Yang

et al. 2015

Electronic Journal of Biotechnology

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Background: Hepcidins, a kind of cysteine-rich antimicrobial peptides, play important roles in host immunological processes and iron regulation, which have been identified from several fish species. The rare minnow (Gobiocypris rarus), an endemic cyprinid fish in China, has been used extensively as model animal in laboratory. However, little is known about its hepcidin. Here, we report the cloning and characterization of a hepcidin gene from the liver of Chinese rare minnow. Results: The full-length cDNA of rare minnow hepcidin is 662 bp, which contains an ORF of 273 bp encoding a prepropeptide of 90 amino acid residues. The predicted prepropeptide contains three domains: a signal peptide of 24 amino acids, a prodomain of 41 amino acids, and a mature peptide of 25 amino acids. Sequence alignment showed eight conserved cysteine residues in the mature peptide, which formed four disulfide bonds in spatial structure. The deduced structure of mature peptide showed a high degree of homology to the human hepcidin. Phylogenetic analysis showed that it had a close relationship with zebrafish hepcidin, and clustered in a clade with these from Cyprinidae. Synthetic peptide of rare minnow hepcidin could inhibit the growth of Gram positive bacterium Staphylococcus aureus and Gram negative bacteria Escherichia coli and Aeromonas hydrophila. Conclusion: These results suggested that rare minnow hepcidin had typical structure of hepcidins and antibacterial activity. It could participate in innate immune response as an antibacterial agent and be used as antibiotic substance.

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Importance of the disulfide bridges in the antibacterial activity of human hepcidin

Cited by 57 publications

References 27 publications

Antimicrobial Peptides from Fish

Antimicrobial Peptides from Fish

Hepcidin Bound to α2-Macroglobulin Reduces Ferroportin-1 Expression and Enhances Its Activity at Reducing Serum Iron Levels

Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)

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