Method for analyzing linear epitopes of vegetable food allergens based on bioinformatics
A bioinformatics, food allergy technology, applied in bioinformatics, informatics, sequence analysis, etc., can solve problems such as high blindness, heavy workload, and difficulty in ensuring accuracy
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Embodiment 1
[0042] The peanut allergen Ara h1 is a 7S globulin and belongs to the Cupin superfamily. Serological analysis found that it can be recognized by more than 90% of peanut allergic patients. Because the structural sequence of the Cupin superfamily has the characteristics of high conservation, strong thermal stability, resistance to enzymatic hydrolysis and indigestibility, Ara h1 was selected as the model allergen in the present invention.
[0043] This embodiment provides a method for analyzing the linear epitope of peanut allergen Ara h1 based on bioinformatics, including the following steps:
[0044] (1) Obtain the complete amino acid sequence of Ara h 1 from the Uniprot database; obtain the 23 linear epitope sequences of Ara h 1 from the allergenic protein structure database SDAP, as shown in Table 1.
[0045] Table 1 Linear epitope sequence of peanut major allergen Ara h 1
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[0048] Note: The key amino acid residues of the IgE binding polypeptide are underlined.
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Embodiment 2
[0057] The walnut allergen Jug r 2 belongs to the 7S pea globulin family, which is the same family as the peanut allergen Ara h1. The primary sequence is composed of 593 amino acids and the molecular weight is about 44kDa.
[0058] This embodiment provides a method for analyzing the linear epitope of walnut allergen Jug r 2 based on bioinformatics, which includes the following steps:
[0059] (1) Homologous modeling prediction of Jug r 2 tertiary structure
[0060] The BLAST search in the PDB database has high homology with the allergen Jug r 2, and the protein sequence of the tertiary structure data has been analyzed by experiments. The results are as follows Image 6 As shown, the 7S pea globulin with PDB access number 5e1r.1.A has the highest matching degree in terms of sequence similarity and coverage, and was selected as the best template for Jug r 2 modeling. 5e1r.1.A is the crystal structure of the 7S pea globulin food allergen of hickory nut. It has a total length of 426 amin...
Embodiment 3
[0071] Wheat allergen CM16 is a protein with a molecular weight of 17kDa and 143 amino acids. It belongs to the gliadin superfamily and contains multiple cysteine residues, which can form intramolecular disulfide bonds to ensure the structural stability of the protein. Has heat resistance.
[0072] This embodiment provides a method for analyzing the linear epitope of wheat allergen CM16 based on bioinformatics, including the following steps:
[0073] (1) Prediction of CM16 linear epitope
[0074] Obtain the amino acid sequence of wheat allergen CM16 from the Uniprot database, use the Hoop-woods amino acid hydrophilicity analysis program in the bioinformatics software DNAStar Protean, the solvent accessibility algorithm of Emini-Surface Probability, the plasticity analysis of Kparlus-Schuzl and Jameson-Wolf's antigen index analysis program analyzes possible linear epitopes of CM16.
[0075] The result is Picture 11 As shown, in the amino acid hydrophilicity analysis, the hydrophili...
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