Gene cloning for vaccine in Pneumocystis carinii pneumonia
| Project/Area Number |
02454243
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Respiratory organ internal medicine
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| Research Institution | The Faculty of Mdedicine, Kagoshima University |
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Principal Investigator |
TANABE Kiyokatsu The Faculty of Medicine, Kagoshima University. Assistant Prof., 医学部, 助教授 (80134625)
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| Project Period (FY) |
1990 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥4,300,000 (Direct Cost: ¥4,300,000)
Fiscal Year 1991: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1990: ¥2,700,000 (Direct Cost: ¥2,700,000)
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| Keywords | PNEUMOCYSTIS CARINII / GENE CLONING / OPPORTUNISTIC INFECTION / VACCINE / 組換えDNA / 後天性免疫不全症候群 / ニュ-モシスチス・カリニ |
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| Research Abstract |
Pneumocystis carinii is a pathogen which causes fatal pneumonia in patients with acquired immune deficiency syndrome. To facilitate the basic study of P. carinii, we analyzed the major surface proteins by immunochemical and biochemical methods. The major protein components of both cvysts (resting form) and trophozoites (vegetative form) are part of a group of proteins called P115 with apparent masses of 105 to 120 kilodaltons. They represent an unusually large portion of the total proteins of this organism. The purified proteins exhibited six isoelectric variants when analyzed by two-dimensional gel electrophoresis. A monoclonal antibody raised against cysts recognized all six variants and reacted with epitopes that were located in the cell wall, thereby indicating that P115 is an immunoreactive surface component. Data are presented that the isoelectirc variants contain identical or clo sely related protein components and that they are mannose-rich glycoproteins. Deglycosylated P115 mi
… More
grates primarily as a single more acidic protein in two-dimensional gels, suggesting that the isoelectric variants may be due primarily to differences in glycosylation. The majority of sera tested from humans with diagnosed pneumocystosis reacted strongly with the P115 proteins.
Several investigators have constructed murine monoclonal antibodies against Pneumocystis carinii. Immunoreactive molecules to these antibodies were various antigens with molecular weights ranging from 35 to 116kDa (Gigliotti et al. 1986 ; Graves et al. 1986 ; Lee et al. 1986 ; Walzer and Linke 1987). We raised another type of monoclonal antibody that reacts with 37- and 32-kDa molecules.
It has been reported that 115-kDa glycoprotein is a major component of cell walls in both cysts and trophozoites (Tanabe et al. 1989). In the present study, 3B7 antibody reacted with 37- and 32kDa molecules but not with the 115-kDa molecule. In addition, 37- and 32-kDa molecules were shown to belocated on the intracytoplasmic organelles. This suggests that these molecules are different from the 115-kDa molecule. Less
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Report
(3 results)
Research Products
(9 results)
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[Publications] Tanake, K., Taklasaki, S., Watanabe, J., Kobata, A., Egawa, K., & Nakamura, Y.: "Glycoproteins composed of major surface immuno determinants of Pneumocystis carinii." Inf. Immu.57. 1363-1368 (1989)
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