Creation of the tailor-made system for antibody production by using an autoantigenic complex
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 |
Research Field |
Functional biochemistry
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Research Institution | Niigata University |
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 |
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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Report
(4 results)
Research Products
(42 results)
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[Journal Article] Solution structure of human P1-P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome2013
Author(s)
Lee, K.M., Yusa, K., Chu, L.O., Yu, C.W., Oono, M., Miyoshi, T., Ito, K., Shaw, P.C., Wong, K.B., and Uchiumi, T
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Journal Title
Nucleic Acids Res
Volume: 41
Issue: 18
Pages: 8776-8787
DOI
Related Report
Peer Reviewed
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[Journal Article] Archaeal ribosomal stalk protein interacts with translation factors in a nucleotide-independent manner via its conserved C terminus2012
Author(s)
Nomura, N., Honda, T., Baba, K., Naganuma, T., Tanzawa, T., Arisaka, F., Noda, M., Uchiyama, S., Tanaka, I., Yao, M., and Uchiumi T
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Journal Title
Proc. Natl. Acad. Sci. U S A
Volume: 109
Pages: 3748-3753
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Peer Reviewed
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[Presentation] The ribosome has multiple "arm-like" structures to catch translation factors2013
Author(s)
Uchiumi, T., Baba, K., Onozuka, M., Honda, T., Nomura, N., and Yao, M
Organizer
International Conference on Nucleic Acid Enzymes and Enzymes in Human Diseases
Place of Presentation
The Chinese University of Hong Kong, Hong Kong
Related Report
Invited
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[Presentation] The ribosome has multiple “arm-like” structures to catch translation factors2013
Author(s)
Uchiumi, T., Baba, K., Onozuka, M., Honda, T., Nomura, N., and Yao, M.
Organizer
International Conference on Nucleic Acid Enzymes and Enzymes in Human Diseases
Place of Presentation
The Chinese University of Hong Kong, Hong Kong
Related Report
Invited
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[Book] 生化学2013
Author(s)
内海利男、馬場健太朗、小野塚美穂
Total Pages
8
Publisher
日本生化学会
Related Report
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