| Project/Area Number |
23657087
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
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| Research Institution | Niigata University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
ITO Koshuke 新潟大学, 自然科学系, 助教 (20502397)
AOYAGI Yutaka 新潟大学, 医歯学系, 教授 (00142266)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | リボソーム / 抗P自己抗体 / 自己抗原 / P蛋白質 / 自己免疫 / 抗体産出系 / 抗リボソーム抗体 / 国際情報交換、香港 / 抗原抗体反応 / P1/P2 / リボソームタンパク質 / 抗Ｐ自己抗体 / ストーク複合体 / 抗原・抗体反応 |
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| Research Abstract |
The aim of this study is to clarify the relationship between the structure and antigenicity of ribosomal autoantigen (P0-P1-P2 complex), and to develop a useful antibody-production system. Epitope analysis of the ribosomal autoantigen identified the 3 amino acids at the C-terminus, which is shared by P0/P1/P2 and responsible for anti-P recognition. It was also found that phosphorylation at Ser residues adjacent to the 3 amino acids enhanced the anti-P binding, suggesting that phosphorylation of the autoantigen is related to the antigenicity. We also found that aP1, the archaeal homologue of human P1/P2, forms a stable tetramer and that immunization of this tetramer resulted in production of antibodies to the conserved C-terminal part. When the C-terminal amino acid sequence was replaced with a sequence of another ribosomal protein, the antibody specific to the introduced sequence was produced. We thus developed a novel method to produce efficiently the antibody for a desired sequence.
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