Ara h 1 structure is retained after roasting and is important for enhanced binding to IgE

Molecular Nutrition and Food Research

Volumn 56, Issue 11, 2012, Pages 1739-1747

  Nesbit, Jacqueline B ^a   Hurlburt, Barry K ^a   Schein, Catherine H ^b   Cheng, Hsiaopo ^a   Wei, Hui ^c   Maleki, Soheila J ^a  

^a SOUTHERN REGIONAL RESEARCH CENTER   (United States)

^b University of Texas Medical Branch School of Medicine   (United States)

^c WATERS CORPORATION   (United States)

Author keywords

Conformational epitope; Epitope; Food allergens; Immunoglobulin E; Peanut allergy

Indexed keywords

ARA H 1 PROTEIN, ARACHIS HYPOGAEA; EPITOPE; GLYCOPROTEIN; IMMUNOGLOBULIN E; PLANT ANTIGEN; VEGETABLE PROTEIN;

ADULT; AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CHILD; CIRCULAR DICHROISM; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; FOOD HANDLING; HEAT; HUMAN; IMMUNOBLOTTING; IMMUNOLOGY; MALE; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; PEANUT; PRESCHOOL CHILD; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE;

ADULT; AMINO ACID SEQUENCE; ANTIGENS, PLANT; ARACHIS HYPOGAEA; CHILD; CHILD, PRESCHOOL; CIRCULAR DICHROISM; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; FEMALE; FOOD HANDLING; GLYCOPROTEINS; HOT TEMPERATURE; HUMANS; IMMUNOBLOTTING; IMMUNOGLOBULIN E; MALE; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY;

ARA; ARACHIS HYPOGAEA;

EID: 84867956722     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201100815     Document Type: Article

References (49)

1. Burks, A. W., Cockrell, G., Stanley, J. S., Helm, R. M. et al., Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity. J. Clin. Invest 1995, 96, 1715-1721.
2. Koppelman, S. J., Vlooswijk, R. A., Knippels, L. M., Hessing, M. et al., Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world. Allergy 2001, 56, 132-137.
3. Teuber, S. S., Beyer, K., Peanut, tree nut and seed allergies. Curr. Opin. Allergy Clin. Immunol. 2004, 4, 201-203.
4. Maleki, S. J., Kopper, R. A., Shin, D. S., Park, C. W. et al., Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. J. Immunol. 2000, 164, 5844-5849.
5. Shin, D. S., Compadre, C. M., Maleki, S. J., Kopper, R. A. et al., Biochemical and structural analysis of the IgE binding sites on ara h1, an abundant and highly allergenic peanut protein. J. Biol. Chem. 1998, 273, 13753-13759.
6. Barre, A., Borges, J. P., Rouge, P., Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: a structural basis for their IgE-binding cross-reactivity. Biochimie 2005, 87, 499-506.
7. Schein, C. H., Ivanciuc, O., Braun, W., Common physical-chemical properties correlate with similar structure of the IgE epitopes of peanut allergens. J. Agric. Food Chem. 2005, 53, 8752-8759.
8. Chruszcz, M., Maleki, S. J., Majorek, K. A., Demas, M. et al., Structural and immunologic characterization of Ara h 1 - a major peanut allergen. J. Biol. Chem. 2011.
9. Barre, A., Sordet, C., Culerrier, R., Rance, F. et al., Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes. Mol. Immunol. 2008, 45, 1231-1240.
10. Vila, L., Beyer, K., Jarvinen, K. M., Chatchatee, P. et al., Role of conformational and linear epitopes in the achievement of tolerance in cow's milk allergy. Clin. Exp. Allergy 2001, 31, 1599-1606.
11. Burks, A. W., Peanut allergy. Lancet 2008, 371, 1538-1546.
12. National Institutes of Health (NIH). Food allergy: Report of the NIH Expert Panel on Food Allergy Research. (June 4, 2007). http://www3.niaid.nih.gov/topics/foodAllergy/research/ReportFoodAllergy.htm.
13. Maillard, L. C., Gautier, M. A., The reaction of amino acids with sugars: mechanisms of melanoid formation. CR Seances Acad. Sci. 1912, III, 66-68.
14. Adrian, J., The Maillard reaction. IV. Study of the behavior of some amino acids during heat-treatment of protein foods. Ann. Nutr. Aliment 1967, 21, 129-147.
15. el-Kayati, S. M., Fadel, H. H., Abdel Mageed, M., Farghal, S. A., Heat and storage effects on the flavour of peanuts. Nahrung 1998, 42, 416-421.
16. Frangne, R., Adrian, J., The Maillard reaction. V. Enzymatic proteolysis of heated foods and significance of results. Ann. Nutr. Aliment 1967, 21, 163-174.
17. Guan, Y. G., Wang, S. L., Yu, S. J., Yu, S. M. et al., Changes in the initial stages of a glucose-proline Maillard reaction model system influences dairy product quality during thermal processing. J. Dairy Sci. 2012, 95, 590-601.
18. Jaeger, H., Janositz, A., Knorr, D., The Maillard reaction and its control during food processing. The potential of emerging technologies. Pathol. Biol. 2010, 58, 207-213.
19. Nowak-Wegrzyn, A., Fiocchi, A., Rare, medium, or well done? The effect of heating and food matrix on food protein allergenicity. Curr. Opin. Allergy Clin. Immunol. 2009, 9, 234-237.
20. Shahidi, F., Ho, C. T., Process-induced chemical changes in foods. An overview. Adv. Exp. Med. Biol. 1998, 434, 1-3.
21. Su, G., Cui, C., Ren, J., Yang, B. et al., Effect of xylose on the molecular and particle size distribution of peanut hydrolysate in Maillard reaction system. J. Sci. Food Agric. 2011, 91, 2457-2462.
22. Van Lancker, F., Adams, A., De Kimpe, N., Chemical modifications of peptides and their impact on food properties. Chem. Rev. 2011, 111, 7876-7903.
23. Barlovic, D. P., Soro-Paavonen, A., Jandeleit-Dahm, K. A., RAGE biology, atherosclerosis and diabetes. Clin. Sci. 2011, 121, 43-55.
24. Himmele, R., Sawin, D. A., Diaz-Buxo, J. A., GDPs and AGEs: impact on cardiovascular toxicity in dialysis patients. Adv. Perit. Dial. 2011, 27, 22-26.
25. Mosquera, J. A., Role of the receptor for advanced glycation end products (RAGE) in inflammation. Invest Clin. 2010, 51, 257-268.
26. Takeda, S., Sato, N., Rakugi, H., Morishita, R., Molecular mechanisms linking diabetes mellitus and Alzheimer disease: beta-amyloid peptide, insulin signaling, and neuronal function. Mol. Biosyst. 2011, 7, 1822-1827.
27. Thomas, M. C., Advanced glycation end products. Contrib. Nephrol. 2011, 170, 66-74.
28. Yamagishi, S., Role of advanced glycation end products (AGEs) and receptor for AGEs (RAGE) in vascular damage in diabetes. Exp. Gerontol. 2011, 46, 217-224.
29. Chassaigne, H., Norgaard, J. V., Hengel, A. J., Proteomics-based approach to detect and identify major allergens in processed peanuts by capillary LC-Q-TOF (MS/MS). J. Agric. Food. Chem. 2007, 55, 4461-4473.
30. Chung, S. Y., Champagne, E. T., Allergenicity of Maillard reaction products from peanut proteins. J. Agric. Food Chem. 1999, 47, 5227-5231.
31. Ilchmann, A., Burgdorf, S., Scheurer, S., Waibler, Z. et al., Glycation of a food allergen by the Maillard reaction enhances its T-cell immunogenicity: role of macrophage scavenger receptor class A type I and II. J. Allergy Clin. Immunol. 2010, 125, 175-183, e171-111.
32. Vojdani, A., Detection of IgE, IgG, IgA and IgM antibodies against raw and processed food antigens. Nutr. Metab. 2009, 6, 22.
33. Maleki, S. J., Food processing: effects on allergenicity. Curr. Opin. Allergy Clin. Immunol. 2004, 4, 241-245.
34. Maleki, S. J., Chung, S. Y., Champagne, E. T., Raufman, J. P., The effects of roasting on the allergenic properties of peanut proteins. J. Allergy Clin. Immunol. 2000, 106, 763-768.
35. Schmitt, D. A., Nesbit, J. B., Hurlburt, B. K., Cheng, H. et al., Processing can alter the properties of peanut extract preparations. J. Agric. Food Chem. 2010, 58, 1138-1143.
36. Andrade, M. A., Chacon, P., Merelo, J. J., Moran, F., Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 1993, 6, 383-390.
37. Sreerama, N., Woody, R. W., Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 1994, 242, 497-507.
38. Sreerama, N., Woody, R. W., A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 1993, 209, 32-44.
39. Maleki, S. J., Teuber, S. S., Cheng, H., Chen, D. et al., Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts. Allergy 2011, 66, 1522-1529.
40. Soman, K. V., Midoro-Horiuti, T., Ferreon, J. C., Goldblum, R. M. et al., Homology modeling and characterization of IgE binding epitopes of mountain cedar allergen Jun a 3. Biophys J. 2000, 79, 1601-1609.
41. Ivanciuc, O., Oezguen, N., Mathura, V., Schein, C. H. et al., Using property based sequence motifs and 3D modeling to determine structure and functional regions in CASP5 targets. Curr. Med. Chem. 2004, 11, 583-593.
42. Oezguen, N., Zhou, B., Negi, S. S., Ivanciuc, O. et al., Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes. Mol. Immunol. 2008, 45, 3740-3747.
43. Fraczkiewicz, R., Braun, W., Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comp. Chem. 1998, 19, 319-333.
44. Wei, H., Glendhill, A., Maleki S.J., The analysis of allergens in raw and roasted peanuts using nanoACQUITY UPLC and Xevo Q-TOF MS. Water's Application Notes 2010, 1-9.
45. Koppelman, S. J., Bruijnzeel-Koomen, C. A., Hessing, M., de Jongh, H. H., Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J Biol. Chem. 1999, 274, 4770-4777.
46. Maleki, S. J., Hurlburt, B. K., Structural and functional alterations in major peanut allergens caused by thermal processing. J. AOAC Int. 2004, 87, 1475-1479.
47. Blanc, F., Vissers, Y. M., Adel-Patient, K., Rigby, N. M. et al., Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity. Mol. Nutr. Food Res. 2011, 55, 1887-1894.
48. Taheri-Kafrani, A., Gaudin, J. C., Rabesona, H., Nioi, C. et al., Effects of heating and glycation of beta-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. J. Agric. Food Chem. 2009, 57, 4974-4982.
49. Amarasekera, M., Rathnamalala, N., Samaraweera, S., Jina-dasa, M., Prevalence of latex allergy among healthcare workers. Int. J. Occup. Med. Environ. Health 2010, 23, 391-396.