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Living Modified Organism
(LMO)
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Rice containing cedar pollen peptide
EN
7Crp#10
No
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Organization:National Institute of Agrobiological Sciences (NIAS)Phone:Fax:Email:Website: http://www.nias.affrc.go.jp/index_e.html,
For the cedar pollen antigen proteins Cryj I and Cryj II which have been identified as the antigens causing cedar pollen allergy, the T cell epitope (12-19 amino acids), recognized by the cedar allergen specific T cells, has been investigated in detail. Then, based on the idea that if the T-cell epitopes of cedar allergen could be accumulated in the daily ingested rice, "the rice possibly offering the effects of mitigating or curing the Japanese cedar pollinosis by ingestion" could be developed based on the oral immune tolerance phenomenon, the epitope peptide accumulated rice was developed.
Nucleotide sequence to express the part of amino acid sequence contained in the antigen proteins Cryj I and Cryj II in the cedar pollens causing pollen allergy and recognized by the human cedar pollen antigen-specific T cell (hereinafter referred to as “human T cell epitope”.
At a total of seven (7) sites, three (3) in Cryj I and four (4) in Cryj II, the human T-cell epitopes, composed of 12 to 19 amino acid residues in length respectively, have been identified. In order to express the artificial peptide (7Crp) composed of 96 amino acid residues by linking the seven-site epitopes (amino acid sequence), the artificial gene was synthesized in accordance with the amino acid sequence of T cell epitope. For the synthesis, the frequently used codon was selected among the gene cluster which encodes the major rice seed storage proteins.
EN
Nucleotide sequence to express the part of amino acid sequence contained in the antigen proteins Cryj I and Cryj II in the cedar pollens causing pollen allergy and recognized by the human cedar pollen antigen-specific T cell (hereinafter referred to as “human T cell epitope”.
At a total of seven (7) sites, three (3) in Cryj I and four (4) in Cryj II, the human T-cell epitopes, composed of 12 to 19 amino acid residues in length respectively, have been identified. In order to express the artificial peptide (7Crp) composed of 96 amino acid residues by linking the seven-site epitopes (amino acid sequence), the artificial gene was synthesized in accordance with the amino acid sequence of T cell epitope. For the synthesis, the frequently used codon was selected among the gene cluster which encodes the major rice seed storage proteins.
The term “Recipient organism” refers to an organism (either already modified or non-modified) that was subjected to genetic modification, whereas “Parental organisms” refers to those that were involved in cross breeding or cell fusion.
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BCH-ORGA-SCBD-10454-5 Organism Oryza sativa (Rice, ORYSA)Crops
EN
pGTV-35S-HPT
EN
- Agrobacterium-mediated DNA transfer
2.300 kb
|
0.072 kb
|
0.288 kb
|
0.012 kb
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0.650 kb
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0.800 kb
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1.100 kb
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0.000 kb
|
Some of these genetic elements may be present as fragments or truncated forms. Please see notes below, where applicable.
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BCH-GENE-SCBD-46121-4 Seven linked human predominant T-cell epitopes | Cryptomeria japonica (Japanese cedar)Protein coding sequence | Changes in quality and/or metabolite content (Allergens)
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BCH-GENE-SCBD-103765-2 Glutelin gene promoter | Oryza sativa (Rice, ORYSA)Promoter
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BCH-GENE-SCBD-103766-1 Glutelin signal peptide | Oryza sativa (Rice, ORYSA)Transit signal
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BCH-GENE-SCBD-103023-2 KDEL ER retention signalTransit signal
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BCH-GENE-SCBD-103767-1 Glutelin terminator | Oryza sativa (Rice, ORYSA)Terminator
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BCH-GENE-SCBD-100287-7 CaMV 35S promoter | Cauliflower mosaic virus (CaMV)Promoter
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BCH-GENE-SCBD-14991-8 Hygromycin B phosphotransferase gene | Escherichia coli (ECOLX)Protein coding sequence | Resistance to antibiotics (Hygromycin),Selectable marker genes and reporter genes
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BCH-GENE-SCBD-103067-9 Transcript 7 gene 3' untranslated region | Agrobacterium tumefaciens (Agrobacterium)Terminator
EN
EN
- Food
EN
EN
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