2005 Fiscal Year Final Research Report Summary
Identification of the binding domain of Plasmodium falciparum erythrocyte binding protein.
| Project/Area Number |
16390126
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Parasitology (including Sanitary zoology)
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| Research Institution | Ehime University |
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Principal Investigator |
TORII Motomi Ehime University, School of Medicine, Professor, 医学部, 教授 (20164072)
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| Co-Investigator(Kenkyū-buntansha) |
KANEKO Osamu Ehime University, School of Medicine, Associate Professor, 医学部, 助教授 (50325370)
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| Project Period (FY) |
2004 – 2005
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| Keywords | infectious disease / malaria / Plasmodium |
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| Research Abstract |
Invasive form of Plasmodium falciparum malaria parasite possesses microorganelle, called Rhoptry, at its apex, from which erythrocyte binding protein RhopH complex (comprising RhopH1, RhopH2, and RhopH3) is discharged and considered to have essential role, because of the failure of attempt to disrupt gene locus. We showed that this complex binds erythrocyte surface via protein and GPI-anchor dependent manner, but the precise mechanism is still unknown. Thus, in this project, we generated genetically manipulated Plasmodium falciparum, which express a part of RhopH complex fused with GFP and asked if each chimeric protein have erythrocyte binding ability. To this end, we generated 4 parasite lines possessing plasmids which would express 1/3 of RhopH1, 2/3 of RhopH1, full length of RhopH1 fused with GFP, or GFP alone under the rhoptry protein promoter. However, we could observe GFP signal only from parasite for 1/3 of RhopH1 and GFP only. The reason why GFP signal is not detected from parasites with 2/3 or full length of RhopH1 is unknown, but we speculate that this maybe because of the relatively large plasmid size. Interestingly, parasite expressing GFP fused with only signal peptide of the RhopH2 showed rhoptry localization of GFP. This indicates that the default destination of the protein with signal peptide could be rhoptry among multipel microorganelle. Immunoprecipitation against RhopH2 did not co-purify 1/3 of RhopH1 plus GFP, indicating this part is not responsible for the RhopH complex formation. Also, we could not observe erythrocyte binding ability for this 1/3 of RhopH1 chimeric protein, suggesting that this region may not be the binding domain.
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[Journal Article] Apical expression of three RhopH1/Clag proteins as components of the Plasmodium falciparum RhopH complex.2005
Author(s)
Kaneko O, Yim-Lim BYS, Iriko H, Ling IT, Otsuki H, Grainger M, Tsuboi T, Adams JH, Mattei D, Holder AA, Torii M.
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Journal Title
Mol Biochem Parasitol 143(1)
Pages: 20-28
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] The Plasmodium falciparum clag 9 gene encodes a rhoptry protein.2004
Author(s)
Ling IT, Florens L, Dluzewski AR, Kaneko O, Grainger M, Lim BY, Tsuboi T, Hopkins JM, Johnson JR., Torii M, Bannister LH, Yates JR, Holder AA, Mattei D.
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Journal Title
Mol Microb 52(1)
Pages: 107-118
Description
「研究成果報告書概要(欧文)」より
