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Expression and functional analysis of Nile tilapia transferrin receptors (TfRs) in host resistance to pathogenic bacteria and iron ion metabolism.

08:00 EDT 18th March 2020 | BioPortfolio

Summary of "Expression and functional analysis of Nile tilapia transferrin receptors (TfRs) in host resistance to pathogenic bacteria and iron ion metabolism."

Transferrin receptors (TfRs) play an essential role in iron-withholding strategy, and are involved in immune response against bacterial infection. In this study, the transferrin receptor 1 (OnTfR1) and transferrin receptor 2 (OnTfR2) genes are identified and characterized in Nile tilapia (Oreochromis niloticus). The open reading frames of OnTfR1 and OnTfR2 are 2220 and 2343 bp of nucleotide sequence, encoding 739 and 780 amino acids, respectively. The deduced proteins of OnTfR1 and OnTfR2 are highly homologous to those of other species, containing three conserved TfR superfamily domains (PA TfR domain, M28 TfR domain and TfR dimer domain). Expression analyses of OnTfRs in the healthy tilapia reveal that the OnTfR1 and OnTfR2 transcripts are the most abundant in the liver. The in vivo studies show that the expressions of OnTfRs are significantly up-regulate in liver and spleen, following infections of Streptococcus agalactiae and Aeromonas hydrophila. In addition, the in vitro studies reveal that the up-regulations of OnTfR expressions are also significant in monocytes/macrophages and hepatocytes upon the stimulations of S. agalactiae and A. hydrophila. Moreover, the iron ion (Fe) could significantly increase the expressions of OnTfRs in monocytes/macrophages and hepatocytes. Taken together, the present study indicates that OnTfRs may be involved in host defense against bacterial infection and possess the function of combining or transporting iron ions in Nile tilapia.

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Name: Fish & shellfish immunology
ISSN: 1095-9947
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Medical and Biotech [MESH] Definitions

Membrane glycoproteins found in high concentrations on iron-utilizing cells. They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where transferrin without its iron is released.

A class of carrier proteins that bind to TRANSFERRIN. Many strains of pathogenic bacteria utilize transferrin-binding proteins to acquire their supply of iron from serum.

A complex of proteins that forms a receptor for TRANSFERRIN in BACTERIA. Many pathogenic bacteria utilize the transferrin-binding complex to acquire their supply of iron from serum.

A subtype of bacterial transferrin-binding protein found in bacteria. It forms a cell surface receptor complex with TRANSFERRIN-BINDING PROTEIN A.

A subtype of bacterial transferrin-binding protein found in bacteria. It forms a cell surface receptor complex with TRANSFERRIN-BINDING PROTEIN B.

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