Identification, characterization and modulation of ferritin-H in the sub-Antarctic Notothenioid Eleginops maclovinus challenged with Piscirickettsia salmonis

Ferritin is a major iron storage protein essential not only in the infectious process, but also in any circumstance generating oxidative stress. In this study, the cDNA coding sequence of ferritin-H was obtained from the sub-Antarctic Notothenioid fish Eleginops maclovinus through transcriptomic ana...

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Published in:Developmental and comparative immunology Vol. 73; pp. 88 - 96
Main Authors: Martínez, D., Oyarzún, R., Vargas-Lagos, C., Pontigo, J.P., Soto-Dávila, M., Saravia, J., Romero, A., Núñez, J.J., Yáñez, A.J., Vargas-Chacoff, L.
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Published: United States Elsevier Ltd 01-08-2017
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Abstract Ferritin is a major iron storage protein essential not only in the infectious process, but also in any circumstance generating oxidative stress. In this study, the cDNA coding sequence of ferritin-H was obtained from the sub-Antarctic Notothenioid fish Eleginops maclovinus through transcriptomic analysis of the head kidney. This sequence contained a 534 bp open reading frame that coded for a 177 amino acid protein with a molecular weight of 20,786.2 Da and a theoretical pI of 5.56. The protein displayed a region of iron putative response elements in the 5′UTR, two putative ferritin iron-binding region signatures, and seven characteristic amino acids with ferroxidase functions. Phylogenetic analysis related this sequence to ferritin-H sequences of other Antarctic Notothenioid fish, sharing 96.61% similarity. Constitutive gene expression analysis in different organs revealed increased ferritin-H gene expression in the gills, spleen, muscle, and liver. After infection with two bacterial strains of Piscirickettsia salmonis (LF-89 and Austral-005), ferritin-H was differentially expressed depending on bacterial strain and tissue. This study provides relevant information towards understanding the iron metabolism of a sub-Antarctic Notothenioid fish. •Ferritin is a major iron storage protein essential in the infectious process.•Phylogenetic related this sequence to ferritin-H sequences of other Antarctic Notothenioid fish, sharing 96.61% homology.•Ferritin-H was differentially expressed depending on bacterial strain type of P. salmonis and tissue.
AbstractList Ferritin is a major iron storage protein essential not only in the infectious process, but also in any circumstance generating oxidative stress. In this study, the cDNA coding sequence of ferritin-H was obtained from the sub-Antarctic Notothenioid fish Eleginops maclovinus through transcriptomic analysis of the head kidney. This sequence contained a 534 bp open reading frame that coded for a 177 amino acid protein with a molecular weight of 20,786.2 Da and a theoretical pI of 5.56. The protein displayed a region of iron putative response elements in the 5'UTR, two putative ferritin iron-binding region signatures, and seven characteristic amino acids with ferroxidase functions. Phylogenetic analysis related this sequence to ferritin-H sequences of other Antarctic Notothenioid fish, sharing 96.61% similarity. Constitutive gene expression analysis in different organs revealed increased ferritin-H gene expression in the gills, spleen, muscle, and liver. After infection with two bacterial strains of Piscirickettsia salmonis (LF-89 and Austral-005), ferritin-H was differentially expressed depending on bacterial strain and tissue. This study provides relevant information towards understanding the iron metabolism of a sub-Antarctic Notothenioid fish.
Ferritin is a major iron storage protein essential not only in the infectious process, but also in any circumstance generating oxidative stress. In this study, the cDNA coding sequence of ferritin-H was obtained from the sub-Antarctic Notothenioid fish Eleginops maclovinus through transcriptomic analysis of the head kidney. This sequence contained a 534 bp open reading frame that coded for a 177 amino acid protein with a molecular weight of 20,786.2 Da and a theoretical pI of 5.56. The protein displayed a region of iron putative response elements in the 5′UTR, two putative ferritin iron-binding region signatures, and seven characteristic amino acids with ferroxidase functions. Phylogenetic analysis related this sequence to ferritin-H sequences of other Antarctic Notothenioid fish, sharing 96.61% similarity. Constitutive gene expression analysis in different organs revealed increased ferritin-H gene expression in the gills, spleen, muscle, and liver. After infection with two bacterial strains of Piscirickettsia salmonis (LF-89 and Austral-005), ferritin-H was differentially expressed depending on bacterial strain and tissue. This study provides relevant information towards understanding the iron metabolism of a sub-Antarctic Notothenioid fish. •Ferritin is a major iron storage protein essential in the infectious process.•Phylogenetic related this sequence to ferritin-H sequences of other Antarctic Notothenioid fish, sharing 96.61% homology.•Ferritin-H was differentially expressed depending on bacterial strain type of P. salmonis and tissue.
Ferritin is a major iron storage protein essential not only in the infectious process, but also in any circumstance generating oxidative stress. In this study, the cDNA coding sequence of ferritin-H was obtained from the sub-Antarctic Notothenioid fish Eleginops maclovinus through transcriptomic analysis of the head kidney. This sequence contained a 534 bp open reading frame that coded for a 177 amino acid protein with a molecular weight of 20,786.2 Da and a theoretical pI of 5.56. The protein displayed a region of iron putative response elements in the 5'UTR, two putative ferritin iron-binding region signatures, and seven characteristic amino acids with ferroxidase functions. Phylogenetic analysis related this sequence to ferritin-H sequences of other Antarctic Notothenioid fish, sharing 96.61% similarity. Constitutive gene expression analysis in different organs revealed increased ferritin-H gene expression in the gills, spleen, muscle, and liver. After infection with two bacterial strains of Piscirickettsia salmonis (LF-89 and Austral-005), ferritin-H was differentially expressed depending on bacterial strain and tissue. This study provides relevant information towards understanding the iron metabolism of a sub-Antarctic Notothenioid fish.
Author Vargas-Lagos, C.
Vargas-Chacoff, L.
Romero, A.
Yáñez, A.J.
Saravia, J.
Oyarzún, R.
Núñez, J.J.
Martínez, D.
Soto-Dávila, M.
Pontigo, J.P.
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Keywords Iron
Gene expression
Notothenioid
Eleginops maclovinus
Ferritin
Language English
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Snippet Ferritin is a major iron storage protein essential not only in the infectious process, but also in any circumstance generating oxidative stress. In this study,...
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SubjectTerms 5' Untranslated Regions
Amino acids
Animals
Apoferritins - physiology
Eleginops maclovinus
Ferritin
Ferroxidase
Fish
Fish Diseases - immunology
Fish Diseases - metabolism
Fishes - physiology
Gene expression
Gene sequencing
Gills
H gene
Iron
Iron - metabolism
Kidneys
Liver
Metabolism
Molecular weight
Muscles
Notothenioid
Organs
Oxidative stress
Phylogeny
Piscirickettsia
Piscirickettsia salmonis
Piscirickettsiaceae Infections - veterinary
Polar environments
Proteins
Regulatory sequences
Spleen
Transcriptome
Title Identification, characterization and modulation of ferritin-H in the sub-Antarctic Notothenioid Eleginops maclovinus challenged with Piscirickettsia salmonis
URI https://dx.doi.org/10.1016/j.dci.2017.03.015
https://www.ncbi.nlm.nih.gov/pubmed/28336188
https://www.proquest.com/docview/2024483831
https://search.proquest.com/docview/1881265522
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