MOLECULAR AND ELECTRON MICROSCOPIC ANALYSES OF ANTIGEN PRESENTATION BY TOXOPLASMA-INFECTED CELLS
Project/Area Number |
04670229
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Research Category |
Grant-in-Aid for General Scientific Research (C)
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Allocation Type | Single-year Grants |
Research Field |
寄生虫学(含医用動物学)
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Research Institution | DEPARTMENT OF MEDICAL ZOOLOGY, NAGASAKI UNIVERSITY SCHOOL OF MEDICINE |
Principal Investigator |
YANO Akihiko DEPARTMENT OF MEDICAL ZOOLOGY, NAGASAKI UNIVERSITY SCHOOL OF MEDICINE PROFESSOR, 医学部, 教授 (20135122)
|
Co-Investigator(Kenkyū-buntansha) |
OHNO Shinichi DEPARTMENT OF ANATOMY YAMANASHI MEDICAL UNIVERSITY PROFESSOR, 医学部, 教授 (50109170)
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Project Period (FY) |
1992 – 1993
|
Project Status |
Completed (Fiscal Year 1993)
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Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1993: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1992: ¥1,500,000 (Direct Cost: ¥1,500,000)
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Keywords | Toxoplasma gondii / Antigen presentation / intracellularly infective protozoa / cell membrane fusion / T cell peptide epitope / electron microscopy / quick-freezing and deep-etching / 急速凍結法 / トキソプラズマ感染細胞 / 細胞傷害性T細胞 / 膜融合 / HLA-A2 / Brefeldin A / ペプチドエピトープ |
Research Abstract |
Electron microscopic analysis of Toxoplasma gondii(T.gondii)-infected cells prepared by the combination of quick-freezing with the deep etching or freeze-substitution methods revealed that the outer membrane of T.gondii fused with some parts of the vacuolar membranes of host cells to build up channel-like structures. Work station and cytofluorometry studies detected T.gondii-derived materials in the cytoplasm of T.gondii-infected cells which strongly suggested the direct entry into cells of T.gondii antigens. Naturally processed peptides derived from T.gondii were acid extracted from T.gondii-infected cells and detected by cytotoxic T lymphocytes(CTL) derived from peripheral blood lymphocytes of a patient with chronic toxoplasmosis. This lytic activity of the CTL lines against T.gondii-infected cells pulsed with fractioned HPLC extract from xx-infected cells was restricted by HLA class I molecules. The amino acid sequence of the HLA class I molecule-bound peptide was in part consistent with the predictive algorithm of HLA class I molecule-binding peptide motifs.
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Report
(3 results)
Research Products
(35 results)