| 论文题目: | Molecular charicatization of feline interferon receptor 2. |
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| 作者: | Qinghua Xue, Limin Yang, Xiaoling Liu, Wenjun Liu* |
| 联系作者: | 刘文军 |
| 刊物名称: | Journal of Interferon and Cytokine Research |
| 期: | 2 |
| 卷: | 30 |
| 页: | 81-88 |
| 年份: | 2010 |
| 影响因子: | 1.774 |
| 论文下载: | 下载地址 |
| 摘要: | The cDNA sequence of feline interferon receptor 2 (feIFNAR2) was generated using RT-PCR method in present study. This gene included 1,572 bp and encoded a 523 aminoacid (aa) protein with a 35 aa signal peptide. The deduced protein shared 61% amino acid identity to the human IFNAR2. There were two fibronectin type III (FBN-III) domains of about 110 residues in the extracellular domain. Homology modeling of feIFNAR2 presented a similar structure with other IFN receptors. The ELISA and FACS experiments demonstrated that the protein could bind to feIFN-alpha or feIFN-omega. However, antiviral activity assay found that feIFN-omega had broader species spectrum compared with feIFN-alpha. To define the functional differences, several point mutations of feIFNAR2 were constructed and the relative affinities of feIFN-a or feIFN-omega for feIFNAR2 and mutants were evaluated. The results suggested that feIFN-alpha and feIFN-omega had different binding sites on feIFNAR2. T75 and M77 on feIFNAR2 were hotspots for binding to feIFN-alpha, but not to feIFN-omega. These findings suggested that the cloned feline IFNAR2 interacted with both feIFN-alpha and feIFN-omega, however, not sharing the same binding sites. |
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