Identification, characterization and modulation of ferritin-H in the sub-Antarctic Notothenioid Eleginops maclovinus challenged with Piscirickettsia salmonis. (August 2017)

• Record Type: Journal Article
• 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.
• Is Part Of: Developmental and comparative immunology. Volume 73(2017)
• Page Start: 88
• Page End: 96
• Publication Date: 2017-08
• Subjects: Eleginops maclovinus -- Ferritin -- Gene expression -- Iron -- Notothenioid; Immunology -- Periodicals; Developmental immunology -- Periodicals; 616.079
• DOI: 10.1016/j.dci.2017.03.015
• Languages: English
• ISSNs: 0145-305X

Abstract

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. Highlights: 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.