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Updated: May 4, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
Published on: July 28, 2014
Two IFNGR1 homologues in Tetraodon nigroviridis: Origin, expression analysis and ligand-binding preference
Dan-Qi Lu1, Ting-Ting Leng1, Xu Ding1
1State Key Laboratory of Biocontrol, Institute of Aquatic Economic Animals and Guangdong Provincial Key Laboratory for Aquatic Economic Animals, College of Life Sciences, Sun Yat-Sen (Zhongshan) University, Guangzhou 510275, PR China.
Abstract:
In the present study, the divergent properties of IFNGR1 isoforms (IFNGR1-1 and IFNGR1-2) were characterized in Tetraodon nigroviridis. Despite the structural similarities between these proteins, two T. nigroviridis IFNGR1 homologues differ from each other not only in their primary nucleotide and amino acid sequences but also in their syntenic structure. Genomic analysis demonstrates the conservation of synteny between the fish IFNGR1-2s and IFNGR1s in higher vertebrates; conversely, the IFNGR1-1 has no corresponding conservation of synteny with Gallus gallus and Homo sapiens, suggesting that the two genes were derived from two different origins. Additionally, their different sensitivities to mitogens and recombinant T. nigroviridis IFN-γs were observed. Furthermore, ligand-binding analysis strongly supported the model proposed in Danio rerio, which suggests that IFNGR1-1 is the major component of the IFN-γrel receptor complex; IFN-γ most likely binds to both IFNGR1-2 and IFNGR1-1. This study is a further step towards elucidating the teleostean IFN-γ system, which is different from that in mammals.
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