Peanut (arachis hypogea) allergens

Chemical and Biological Properties of Food Allergens

Volumn , Issue , 2009, Pages 267-280

  Szymkiewicz, Agata ^a  

^a INSTITUTE OF ANIMAL REPRODUCTION AND FOOD RESEARCH   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGENS; ALLERGIES;

ALLERGIC REACTIONS; ARACHIS HYPOGEA; BREAKFAST CEREALS; CLEANING AGENTS; DEVELOPED COUNTRIES; PEANUT ALLERGENS; PEANUT ALLERGIES; PEDIATRIC POPULATION;

OILSEEDS;

EID: 85014780607     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (84)

1. Adachi, M., Takenaka, Y., Gidamis, A.B., Mikami, B., and Utsumi S. 2001. Crystal structure of soybean proglycinin A1aB1b homotrimer. J Mol Biol 305:291–305.
2. Barnett, D., Bonham B., and Howden, M.E.H. 1987. Allergenic cross-reactions among legume foods — An in vitro study. J Allergy Clin Immunol 79:433–438.
3. Barre, A., Borges, J.-P., Culerrier, R., and Rougé, P. 2005a. Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes. Immunol Lett 100:153–158.
4. Barre, A., Borges, J.-P., and Rougé, P. 2005b. 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 87:499–506.
5. Barre, A., Jacquet, G., Sordet, C., Culerrier, R., and Rougé P. 2007. Homology modelling and conformational analysis of IgE-binding epitopes of Ara h 3 and other legumin allergens with a cupin fold from tree nuts. Mol Immunol 44:3243–3255.
6. Bernhisel-Broadbent, J. and Sampson, H.A. 1989. Cross-allergenicity in the legume botanical family in children with food hypersensitivity. J Allergy Clin Immunol 83:435–440.
7. Beyer, K., Morrow, E., Li, X.M. et al. 2001. Effects of cooking methods on peanut allergenicity. J Allergy Clin Immunol 107:1077–1081.
8. Bock, S.A., Atkins, F.M., and Sampson, H.A. 1988. Allergenic cross-reactivity among legume food. J Allergy Clin Immunol 82:310–312.
9. Bonds, R.S., Maleki, S.J., McBride, J., and Cheng, H. 2006. In vitro cross-reactivity of peanut allergens with other legumes. J Allergy Clin Immunol 11:154.
10. Bruijnzeel-Koomen, C., Ortolani, C., Aas, K. et al. 1995. Adverse reactions to food. Position paper. Allergy 50:623–635.
11. Burks, A.W. 2003. Peanut allergy: A growing phenomenon. J Clin Invest 111:950–952.
12. Burks, A.W. 2008. Peanut allergy. Lancet 371:1538–1546.
13. Burks, A.W., Williams, L.W., Helm, R.M., Connaughton, C., Cocrel, LG., and O’Brien, T.J. 1991. Identification of a major peanut allergen, Ara h 1, in patients with atopic dermatitis and positive peanut challenges. J Allergy Clin Immunol 88:72–179.
14. Burks, A.W., Williams, L.W., Connaughton, C., Cocrell, G., O’Brien, T.J., and Helm, R.M. 1992. Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenges. J Allergy Clin Immunol 90:962–969.
15. Burks, A.W., Cockrell, G., Connaughton, C., and Helm, R.M. 1994. Epitope specificity and immunoaffinity purification of the major peanut allergen, Ara h 1. J Allergy Clin Immunol 93:743–750.
16. Burks, A.W., Cocrell, G., Stanley, J.S., Helm, R.M., and Bannon, G.A. 1995. Recombinant peanut allergen Ara h 1 expression and IgE-binding in patients with peanut hypersensitivity. J Clin Invest 96:1715–1721.
17. Burks, A.W., Shin, D., Cockrell, G., Stanley, J.S., Helm, R.M., and Bannon, G.A. 1997. Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. Eur J Biochem 245:334–339.
18. Burks, A.W., Sampson, H.A., and Bannon, G.A. 1998. Review Article Series II. Peanut allergens. Allergy 53:725–730.
19. Chatel, J.M., Bernard, H., and Orson, F.M. 2003. Isolation and characterization of two complete Ara h 2 isoforms cDNA. Int Arch Allergy Immunol 131:14–18.
20. Clement, G., Boquet, D., Mondoulet, L., Lamourette, P., Bernard, H., and Wal, J.M. 2005. Expression in Escherichia coli and disulfide bridge mapping of PSC33, an allergenic 2S albumin from peanut. Protein Expr Purif 44:110–120.
21. Crespo, J.F., Rodriguez, J., Vives, R. et al. 2001. Occupational IgE-mediated allergy after exposure to lupine seed flour. J Allergy Clin Immunol 108:295–297.
22. Duranti, M. and Gius, C. 1997. Legume seeds: Protein content and nutritional value. Field Crops Res 53:31–45.
23. Eigenmann, P.A., Burks, A.W., Bannon, G.A., and Sampson, H.A. 1996. Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies. J Allergy Clin Immunol 98:969–978.
24. Emmett, S.E., Angus, F.J., Fry, J.S., and Lee, P.N. 1999. Perceived prevalence of peanut allergy in Great Britain and its association with other atopic conditions and with peanut allergy in other household members. Allergy 54:380–385.
25. Furlong, T.J., DeSimone, J., and Sicherer, S.H. 2001. Peanut and tree nut allergic reactions in restaurants and other food establishments. J Allergy Clin Immunol 108:867–870.
26. Hefle, S.L., Lemanske, R.F.J., and Bush, R.K. 1994. Adverse reaction to lupine-fortified pasta. J Allergy Clin Immunol 94:167–172.
27. Hourihane, J.B., Aiken, R., Briggs, R. et al. 2007. The impact government advice to pregnant mothers regarding peanut avoidance on the prevalence of peanut allergy in United Kingdom children at school entry. J Allergy Clin Immunol 119:1197–1202.
28. Huang, A.H.C. 1992. Oil bodies and oleosins in seed. Ann Rev Plant Physiol Plant Mol Biol 43:177–200.
29. Huang, A.H.C. 1996. Oleosins and oil bodies in seed of other organs. Plant Physiol 110:1055–1061.
30. Ibanˇ ez, D., Martinez, M., Sanchez, J.J., and Fernández-Caldas, E. 2003. Legume: Crossreactivity. Allergol Immunopathol 31:151–161.
31. Jensen-Jarolim, E., Wiedermann, U., Ganglberger, E. et al. 1999. Allergen mimotopes in food enhance type I allergic reactions in mice, FASEB J 13:1586–1592.
32. Kang, I.-K. and Gallo, M. 2007. Cloning and characterization of a novel peanut allergen Ara h 3 isoform displaying potentially decreased allergenicity. Plant Sci 172: 345–353.
33. Kilanowski, J., Stalter, A.M., and Gottesman, M.M. 2006. Preventing peanut panic. J Pediatr Health Care 20:61–66.
34. Kleber-Janke, T., Crameri, R., Appenzeller, U., Schlaak, M., and Becker, W.M. 1999. Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int Arch Allergy Immunol 119:265–274.
35. Kleber-Janke, T., Crameri, R., Scheurer, S., Vieths, S., and Becker, W. 2001. Patient-tailored cloning of allergens by phage display: Peanut (Arachis hypogaea) profiling, a food allergen derived from a rare mRNA. J Chromatogr B 756:295–305.
36. Ko, T.P., Day, J., and McPerson, A. 2000. The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 Å resolution. Acta Crystallogr D 56:411–420.
37. Koppelman, S.J., Knol, E.F., Vlooswijk, R.A.A. et al. 2003. Peanut allergen Ara h 3: Isolation from peanuts and biochemical characterization. Allergy 58:1144–1151.
38. Koppelman, S.J., Wensing, M., Ertmann, M., Knulst, A.C., and Knol, E.F. 2004. Relevance of Ara h1, Ara h 2, and Ara h 3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h 2 is the most important peanut allergen. Clin Exp Allergy 34:583–590.
39. Lawrence, M.C., Izard, T., Beuchat, M., Blagrove R.J., and Colman, P.M. 1994. Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin and the genetic engineering of seed storage proteins. J Mol Biol 238:748–776.
40. Lehmann, K., Schweimer, K., Neudecker, P., and Rosch, P. 2004. Sequence-specific 1H, 13C and 15N resonance assignments of Ara h 6, an allergenic 2S albumin from peanut. J Biomol NMR 29:93–94.
41. Lifrani, A., Dubarry, M., Rautureau, M., Aattouri, N., Boyaka, P.N., and Tome, D. 2005. Peanut-lupine antibody cross-reactivity is not associated to cross-allergenicity in peanut-sensitized mouse strains. Int Immunopharmacol 5:1427–1435.
42. Long, A. 2002. The bolts of peanut allergy. N Engl J Med 346:1320–1322.
43. Makri, E., Papalamprou, E., and Doxastakis, G. 2005. Study of functional properties of seed storage proteins from indigenous European legume crops (lupin, pea, broad bean) in admixture with polysaccharides. Food Hydrocoll 19:583–594.
44. Maleki, S.J., Chung, S., Champagne, E.T., and Raufman, J.P. 2000a. The effects of processing and the allergenic properties of peanut proteins. J Allergy Clin Immunol 106:763–776.
45. Maleki, S.J., Kopper, R.A., Shin, D.S. et al. 2000b. Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. J Immunol 164:5844–5849.
46. Maleki, S.J., Chung, S., Champagne, E.T., and Raufman, J.P. 2001. Allergic and biophysical properties of peanut proteins before and after roasting. Food Allergy Tolerance 2:211–221.
47. Maleki, S.J., Viquez, O., Jacks, T. et al. 2003. The major peanut allergen, Ara h 2, functions as trypsin inhibitor, and roasting enhances this function. J Allergy Clin Immunol 112:190–195.
48. Maloney, J.M., Chapman, M.D., and Sicherer, S.H. 2006. Peanut allergen exposure through saliva: Assessment and interventions to reduce exposure. J Allergy Clin Immunol 118:719–724.
49. Markovic-Housley, Z., Degano, M., Lamba, D. et al. 2003. Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. J Mol Biol 325:123–133.
50. Matheu, V., de Barrio, M., Sierra, Z., Gracia-Bara, M.T., Tornero, P., and Baeza, M.L. 1999. Lupine-induced anaphylaxis. Ann Allergy Asthma Immunol 83:406–408.
51. Mittag, D., Akkerdaas, J., Ballmer-Weber, B. et al. 2004a. Ara h 8 a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J Allergy Clin Immunol 114:1410–1417.
52. Mittag, D., Vieths, S., Vogel, L. et al. 2004b. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol 113:148–154.
53. Moneret-Vautrin, D.A., Guérin, L., Kanny, G., Flabbee, J., Frémont, S., and Morisset, M. 1999. Cross-allergrenicity of peanut and lupine: The risk of lupine allergy in patients allergic to peanuts. J Allergy Clin Immunol 104:883–888.
54. Moreno-Ancillo, A., Gil-Adrados, A.C., Dominguez-Noche, C., and Cosmes, P.M. 2005. Lupine inhalation induced asthma in a child. Pediatr Allergy Immunol 16:542–544.
55. Novembre, E., Moriondo, M., Bernardini, R., Rossi, M.E., and Vierucci A. 1999. Lupine allergy in a child. J Allergy Clin Immunol 103:1214–1216.
56. Palmer, G.W., Dibbern, D.A., Burks. et al. 2005. Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity. Clin Immunol 115:302–312.
57. Parisot, L., Aparicio, C., Moneret-Vautrin, D.A., and Guerin, L. 2001. Allergy to lupine flour. Allergy 56:918–919.
58. Pascual, C.Y., Fernandez-Crespo, J., Sanchez-Pastor, S. et al. 1999. Allergy to lentils in Mediterranean paediatric patients. J Allergy Clin Immunol 103:154–158.
59. Patil, S.P., Niphadkar, P.V., and Bapat, M.M. 2001. Chickpea: A major food allergen in the Indian subcontinent and its clinical and immunochemical correlation. Ann Allergy Asthma Immunol 87:140–145.
60. Peeters, K.A.B.M., Kunlst, A.C., Rynja, F.L., Bruijnzeel-Koomen, C.A.F.M., and Koppelman, S.J. 2004. Peanut allergy: Sensitization by peanut oil-containing local therapeutics seems unlikely. J Allergy Clin Immunol 113:1000–1001.
61. Peeters, K.A.B.M., Nordlee, J.A., Penninks, A.H. et al. 2007. Lupine allergy: Not simply cross-reactivity with peanut or soy. J Allergy Clin Immunol 120:647–653.
62. Perry, T.T., Conover-Walker, M.K., Pomes, A., Chapman, D.M., and Wood, R.A. 2004. Distribution of peanut allergen in the environment. J Allergy Clin Immunol 113:973–976.
63. Pomés, A., Helm, R.M., Bannon, G.A., Burks, A.W., Tsay, A., and Chapman, M.D. 2003. Monitoring peanut allergen in food products by measuring Ara h 1. J Allergy Clin Immunol 111:640–645.
64. Pomés, A., Vinton, R., and Chapman, M.D. 2004. Peanut allergen (Ara h 1) detection in foods containing chocolate. J Food Prot 67:793–798.
65. Pons, L., Chéry, C., Mrabet, N., Schohn, H., Lapicque, F., and Guéant, J.-L. 2005. Purification and cloning of two high molecular mass isoforms of peanut seed oleosin encoded by cDNAs of equal sizes. Plant Physiol Biochem 43:659–668.
66. Rabjohn, P., Helm, R.M., Stanley, J.S. et al. 1999. Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J Clin Invest 103:535–542.
67. Radcliffe, M., Scadding, G., and Brown, H.M. 2005. Lupine flour anaphylaxis. Lancet 365:1360–1360.
68. Restani, P., Ballabio, C., Corsini, E. et al. 2005. Identification of the basic subunit of Ara h 3 as the major allergen in a group of children allergic to peanuts. Ann Allergy Asthma Immunol 94:262–266.
69. Sampson, H.A. 2003. Anaphylaxis and emergency treatment. Pediatrics 111:1601–1608.
70. Sen, M., Kopper, R., Pons, L., Abraham, E.C., Burks, A.W., and Bannon, G.A. 2002. Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J Immunol 169:882–887.
71. Shin, D.S., Compadre, C.M., Maleki, S.J. et al. 1998. Biochemical and structural analysis of the IgE-binding sites on Ara h 1, an abundant and highly allergenic peanut protein. J Biol Chem 273:13753–13759.
72. Shreffler, W.G., Beyer, K., Chu, T.H., Burks, A.W., and Sampson, H.A. 2004. Microarray immunoassay: Association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes. J Allergy Clin Immunol 113:776–782.
73. Sicherer, S.H., Munoz-Furlong, A., Burks, A.W., and Sampson, H.A. 1999. Prevalence of peanut and tree nut allergy in the US determined by a random digit dial telephone survey. J Allergy Clin Immunol 103:559–562.
74. Sicherer, S.H., Muñoz-Furlong, A., Burks, A.W., and Sampson, H.A. 2003. Prevalence of peanut and tree nut allergy in the United States determined by means of random digit dial telephone survey: A 5-year follow-up study. J Allergy Clin Immunol 112:1203–1207.
75. Sicherer, S.H., Sampson, H.A., and Burks, A.W. 2000. Peanut and soy allergy: A clinical and therapeutic dilemma – Review. Allergy 55:515–521.
76. Stanley, J.S., King, N., Burks, A.W. et al. 1997. Identification mutational analysis of the immunodominant IgE-binding epitopes of the major peanut allergen Ara h 2. Arch Biochem Biophys 342:244–253.
77. van Ree, R., Cabanes-Macheteau, M., Akkerdaas, J. et al. 2000. Beta(1,2)-xylose and alpha(1,3)-fucose residues have a strong contribution in IgE-binding to plant glycoallergens. J Biol Chem 275:11451–11458.
78. Vieths, S., Reindl, J., Muller, U., Hoffmann, A., and Haustein, D. 1999. Digestability of peanut and hazelnut allergens investigated by a simple in vitro procedure. Eur Food Res Technol 209:379–388.
79. Vieths, S., Scheurer, S., and Ballmer-Weber, B. 2002. Current understanding of cross- reactivity of food allergens and pollen. Ann N Y Acad Sci 964:47–68.
80. Woo, E.J., Dunwell, J.M., Goodenough, P.W., Marvier, A.C., and Pickersgill R.W. 2000. Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nat Strut Biol 7:1036–1040.
81. Wensing, M., Knulst, A.C., Piersma, S., O’Kane, F., Knol, E.F., and Koppelman, S.J. 2003. Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h1). J Allergy Clin Immunol 111:420–424.
82. Wensing, M., Penninks, A.H., Hefle, S.L., Koppelman, S.J., Bruijnzeel-Koomen, C.A.F.M., and Knulst, A.C. 2002. The distribution of individual threshold doses eliciting allergic reactions in a population with peanut allergy. J Allergy Clin Immunol 110:915–920.
83. Xiang, P., Beardslee, T.A., Zeece, M.G., Markwell, J., and Sarath, G. 2002. Identification and analysis of a conserved immunoglobulin E-binding epitope in soybean G1a and G2a and peanut Ara h 3 glycinins. Arch Biochem Biophys 408:51–57.
84. Yu, J.W., Kagan, R., Verreault, N. et al. 2006. Accidental ingestions in children with peanut allergy. J Allergy Clin Immunol 118:466–472.