Identification of Antibacterial Activity of Hepcidin From Antarctic Notothenioid Fish
Hepcidin is a small peptide composed of signal peptide, propeptide, and the bioactive mature peptide from N terminal to C terminal. Mature hepcidin is an antibacterial peptide and iron regulator with eight highly conserved cysteines forming four intramolecular disulfide bonds, giving it a β sheet ha...
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ftdoajarticles:oai:doaj.org/article:38e933c43bdf4333bdd688e9fd41246e 2023-05-15T13:45:15+02:00 Identification of Antibacterial Activity of Hepcidin From Antarctic Notothenioid Fish Mingli Liu Ruiqin Hu Wenhao Li Wenyi Yang Qianghua Xu Liangbiao Chen 2022-04-01T00:00:00Z https://doi.org/10.3389/fmicb.2022.834477 https://doaj.org/article/38e933c43bdf4333bdd688e9fd41246e EN eng Frontiers Media S.A. https://www.frontiersin.org/articles/10.3389/fmicb.2022.834477/full https://doaj.org/toc/1664-302X 1664-302X doi:10.3389/fmicb.2022.834477 https://doaj.org/article/38e933c43bdf4333bdd688e9fd41246e Frontiers in Microbiology, Vol 13 (2022) hepcidin Antarctic notothenioid fish antibacterial peptide recombinant protein antibacterial activity Microbiology QR1-502 article 2022 ftdoajarticles https://doi.org/10.3389/fmicb.2022.834477 2022-12-30T22:03:12Z Hepcidin is a small peptide composed of signal peptide, propeptide, and the bioactive mature peptide from N terminal to C terminal. Mature hepcidin is an antibacterial peptide and iron regulator with eight highly conserved cysteines forming four intramolecular disulfide bonds, giving it a β sheet hairpin-like structure. Hepcidin homologs are found in a variety of vertebrates, especially fish, and their diversity may be associated with different habitats and different levels of pathogens. Dissostichus mawsoni, an Antarctic notothenioid fish that lives in the coldest water unlike most places of the world, with at least two hepcidin variants with eight cysteines. We confirmed the formation process of activated mature hepcidins from D. mawsoni in Chinese hamster ovary (CHO) cell line, obtained recombinant hepcidin protein from prokaryotes, and characterized its binding ability and antibacterial activity against varying bacteria. The expression of hepcidin in CHO cell line showed that the prepropeptide of Dmhep_8cysV1 and Dmhep_8cysV2 cleavage into smaller mature peptide. The antibacterial assay and flow cytometry showed that Dmhep_8cysV1, Dmhep_8cysV2, and Drhep bound to different bacteria and killed them with different minimum inhibitory concentration. These data suggest that hepcidin plays an important role in the innate immunity of D. mawsoni and is of great value in improving resistance to pathogens. Article in Journal/Newspaper Antarc* Antarctic Directory of Open Access Journals: DOAJ Articles Antarctic Frontiers in Microbiology 13 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
hepcidin Antarctic notothenioid fish antibacterial peptide recombinant protein antibacterial activity Microbiology QR1-502 |
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hepcidin Antarctic notothenioid fish antibacterial peptide recombinant protein antibacterial activity Microbiology QR1-502 Mingli Liu Ruiqin Hu Wenhao Li Wenyi Yang Qianghua Xu Liangbiao Chen Identification of Antibacterial Activity of Hepcidin From Antarctic Notothenioid Fish |
topic_facet |
hepcidin Antarctic notothenioid fish antibacterial peptide recombinant protein antibacterial activity Microbiology QR1-502 |
description |
Hepcidin is a small peptide composed of signal peptide, propeptide, and the bioactive mature peptide from N terminal to C terminal. Mature hepcidin is an antibacterial peptide and iron regulator with eight highly conserved cysteines forming four intramolecular disulfide bonds, giving it a β sheet hairpin-like structure. Hepcidin homologs are found in a variety of vertebrates, especially fish, and their diversity may be associated with different habitats and different levels of pathogens. Dissostichus mawsoni, an Antarctic notothenioid fish that lives in the coldest water unlike most places of the world, with at least two hepcidin variants with eight cysteines. We confirmed the formation process of activated mature hepcidins from D. mawsoni in Chinese hamster ovary (CHO) cell line, obtained recombinant hepcidin protein from prokaryotes, and characterized its binding ability and antibacterial activity against varying bacteria. The expression of hepcidin in CHO cell line showed that the prepropeptide of Dmhep_8cysV1 and Dmhep_8cysV2 cleavage into smaller mature peptide. The antibacterial assay and flow cytometry showed that Dmhep_8cysV1, Dmhep_8cysV2, and Drhep bound to different bacteria and killed them with different minimum inhibitory concentration. These data suggest that hepcidin plays an important role in the innate immunity of D. mawsoni and is of great value in improving resistance to pathogens. |
format |
Article in Journal/Newspaper |
author |
Mingli Liu Ruiqin Hu Wenhao Li Wenyi Yang Qianghua Xu Liangbiao Chen |
author_facet |
Mingli Liu Ruiqin Hu Wenhao Li Wenyi Yang Qianghua Xu Liangbiao Chen |
author_sort |
Mingli Liu |
title |
Identification of Antibacterial Activity of Hepcidin From Antarctic Notothenioid Fish |
title_short |
Identification of Antibacterial Activity of Hepcidin From Antarctic Notothenioid Fish |
title_full |
Identification of Antibacterial Activity of Hepcidin From Antarctic Notothenioid Fish |
title_fullStr |
Identification of Antibacterial Activity of Hepcidin From Antarctic Notothenioid Fish |
title_full_unstemmed |
Identification of Antibacterial Activity of Hepcidin From Antarctic Notothenioid Fish |
title_sort |
identification of antibacterial activity of hepcidin from antarctic notothenioid fish |
publisher |
Frontiers Media S.A. |
publishDate |
2022 |
url |
https://doi.org/10.3389/fmicb.2022.834477 https://doaj.org/article/38e933c43bdf4333bdd688e9fd41246e |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Frontiers in Microbiology, Vol 13 (2022) |
op_relation |
https://www.frontiersin.org/articles/10.3389/fmicb.2022.834477/full https://doaj.org/toc/1664-302X 1664-302X doi:10.3389/fmicb.2022.834477 https://doaj.org/article/38e933c43bdf4333bdd688e9fd41246e |
op_doi |
https://doi.org/10.3389/fmicb.2022.834477 |
container_title |
Frontiers in Microbiology |
container_volume |
13 |
_version_ |
1766217751635951616 |