2013 Fiscal Year Final Research Report
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 |
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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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| 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 |
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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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[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
Pages: 8776-8787
DOI
Peer Reviewed
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[Journal Article] Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB82013
Author(s)
Matsumoto, A., Shimizu, Y., Takemoto, C., Ueda, T., Uchiumi, T., and Ito K
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Journal Title
Acta Crystallogr. Sect F
Volume: 69
Pages: 332-335
DOI
Peer Reviewed
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[Journal Article] Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase2012
Author(s)
Ito, K., Murakami, R., Mochizuki, M., Qi, H., Shimizu, Y., Miura, K., Ueda, T., and Uchiumi, T
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Journal Title
Nucleic Acids Res
Volume: 40
Pages: 10521-10531
DOI
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
DOI
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
Year and Date
20130616-21
Invited
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[Presentation] リボソームには複数の"腕"がある2012
Author(s)
内海利男, 野村直子, 本田貴嘉, 馬場健太朗, 長沼孝雄, 田中勲, 姚閔
Organizer
第1回RIBOSOME MEETING
Place of Presentation
広島大学生物生産学部
Year and Date
20120315-16
Invited
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