Elucidation of a synthetic pathway for complex-type N-linked glycans in Trypanosoma brucei
| Project/Area Number |
25460522
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Parasitology (including sanitary zoology)
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| Research Institution | Matsuyama University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2014: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2013: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
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| Keywords | トリパノソーマ原虫 / 糖鎖 / 糖タンパク質 / トリパノソーマ / 原虫 / N-結合型糖鎖 / 糖転移酵素 / Trypanosoma brucei / GnT-I |
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| Outline of Final Research Achievements |
Trypanosoma brucei, a causative parasite of African Sleeping sickness, is thought to require the expression of complex-type N-linked glycans for its proliferation. However, little is known about the responsible enzymes for the glycan synthesis. Especially, lack of a homolog to GnT-I was a mystery for years. This project focused on the identification of the enzyme of T. brucei (TbGnT-I). Although TbGT11 was reported as the TbGnT-I in the middle of this project, it was still not clear whether the enzyme was alone sufficient to catalyze GnT-I activity. We found that native TbGnT-I showed a size of ca. 400 kDa by a gel filtration chromatography, and overexpressed TbGT11HA3 was also contained in the fraction. The recombinant TbGT11HA3 showed no activity when expressed in other than T. brucei. An N-linked glycosylation on TbGT11 was essential for the activity. These results strongly suggested that TbGnT-I was a 400-kDa protein complex containing glycosylated TbGT11 as an essential component.
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Report
(4 results)
Research Products
(8 results)
