Characterization of lupin major allergens (Lupinus albus L.)

Molecular Nutrition and Food Research

Volumn 54, Issue 11, 2010, Pages 1668-1676

  Guillamón, Eva ^a   Rodríguez, Julia ^b   Burbano, Carmen ^a   Muzquiz, Mercedes ^a   Pedrosa, Mercedes M ^a   Cabanillas, Beatriz ^b   Crespo, Jesús F ^b   Sancho, Ana I ^c   Mills, E N Clare ^c   Cuadrado, Carmen ^a  

^a INIA   (Spain)

^b HOSPITAL UNIVERSITARIO 12 DE OCTUBRE   (Spain)

^c NORWICH RESEARCH PARK   (United Kingdom)

Author keywords

Conglutin ; Conglutin ; Food allergens; Lupinus albus

Indexed keywords

ALLERGEN; EPITOPE; GALECTIN 3; IMMUNOGLOBULIN E; SEED STORAGE PROTEIN; VICILIN PROTEIN, PLANT;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CROSS REACTION; FLOUR; FOOD ALLERGY; HUMAN; IMMUNOLOGY; LEGUME; LUPIN; MICROBIOLOGY; MOLECULAR GENETICS; PEANUT; PLANT SEED;

ALLERGENS; AMINO ACID SEQUENCE; ARACHIS HYPOGAEA; CROSS REACTIONS; EPITOPES; FABACEAE; FLOUR; FOOD HYPERSENSITIVITY; GALECTIN 3; HUMANS; IMMUNOGLOBULIN E; LUPINUS; MOLECULAR SEQUENCE DATA; SEED STORAGE PROTEINS; SEEDS;

ARACHIS HYPOGAEA; LUPINUS ALBUS;

EID: 77956522392     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.200900452     Document Type: Article

References (50)

1. Sirtori, C.-R., Lovati, M.-R., Manzoni, C., Castiglioni, S. et al., Proteins of white lupin seed, a naturally isoflavone-poor legume, reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells. J. Nutr. 2004, 134, 18-23.
2. Magni, C., Sessa, F., Accardo, E., Bañón, M. et al., Conglutinγ, a lupin seed protein, binds insulin in vitro and reduces plasma glucose levels of hyperglycemic rats. J. Nutr. Biochem. 2004; 15, 646-650.
3. Marchesi, M., Parolini, C., Diani, E., Rigamonti, E. et al., Hypolipidaemic and anti-atherosclerotic effects of lupin proteins in a rabbit model. Br. J. Nutr. 2008, 100, 707-710.
4. Duranti, M., Restani, P., Poniatowska, M., Cerletti, P., The seed globulins of Lupinus albus. Phytochemistry 1981, 20, 2071-2075.
5. Duranti, M., Consonni, A., Magni, C., Sessa, F. et al., The major proteins of lupin seed: characterization and molecular properties for use as functional and nutraceutical ingredients. Trends Food Sci. Tech. 2008, 19, 624-633.
6. Wait, R., Gianazza, E., Brambilla, D., Eberini, I. et al., Analysis of Lupinus albus storage proteins by two-dimensional electrophoresis and mass spectrometry. J. Agric. Food Chem. 2005, 53, 4599-4606.
7. Hefle, S.-L., Lemanske, R.-F., Bush, R.-K., Adverse reaction to lupine-fortified pasta. J. Allergy Clin. Immunol. 1994, 94, 167-172.
8. Romano, C., Ferrara, A., Tarallo, S., Allergic reaction to lupine seed (Lupinus albus). Allergy 1997, 2, 113-114.
9. Matheu, V., de Barrio, M., Sierra, Z., Azzari, C. et al., Lupine-induced anaphylaxis. Ann. Allergy Asthma Immunol. 1999, 83, 406-408.
10. Magni, C., Ballabio, C., Restani, P., Sironi, E. et al., Two-dimensional electrophoresis and western-blotting analyses with anti Ara h 3 Basic subunit IgG evidence the cross-reacting polypeptides of Arachis hypogaea, Glycine max and Lupinus albus seed proteomes. J. Agric. Food Chem. 2005, 53, 2275-2281.
11. Moneret-Vautrin, D.-E., Guerin, L., Kanny, G., Flabbee, J. et al., Cross-allergenicity of peanut and lupine: the risk of lupine allergy in patients allergic to peanuts. J. Allergy Clin. Immunol. 1999, 104, 883-888.
12. Fæste, C.-K., Løvik, M., Wiker, H.-G., Egaas, E., A case of peanut cross-allergy to lupine flour in a hot dog bread. Int. Arch. Allergy Immunol. 2004, 135, 36-39.
13. Radcliffe, M.-J., Scadding, G.-K., Morrow-Brown, H., Lupin flour anaphylaxis. Lancet 2005, 365, 1360.
14. Lindvik, H., Holden, L., Levik, M., Cvancarova, M. et al., Lupin sensitisation and clinical allergy in food allergic children in Norway. Acta Paeditrica 2008, 97, 91-95.
15. Shaw, J., Roberts, G., Grimshav, K., White, S. et al., Lupin allergy in peanut-allergic children and teenagers. Allergy 2008, 63, 370-373.
16. Crespo, J.-F., Rodríguez, J., Vives, R., James, J.-M. et al., Occupational IgE-mediated allergy after exposure to lupine seed flour. J. Allergy Clin. Immunol. 2001, 56, 918-919.
17. European Commission. Commission Directive 2007/68/EC of 27 November 2007 amending Annex IIIa to Directive 2000/13/EC of the European Parliament and of the Council as regards certain food ingredients. Off. J. Eur. Union 2007, L310/11.
18. Peeters, K.-A., Nordlee, J.-A., Penninks, A.-H., Chen, L. et al., Lupine allergy: not simply cross-reactivity with peanut or soy. J. Allergy Clin. Immunol. 2007, 120, 647-653.
19. Magni, C., Herndl, A., Sironi, E., Scarafoni, A. et al., One- and two-dimensional electrophoretic identification of IgE-binding polypeptides of Lupinus albus and other legume seeds. J. Agric. Food Chem. 2005, 53, 4567-4571.
20. Goggin, D.-E., Mir, G., Smith, W.-B., Stuckey, M. et al., Proteomic analysis of lupin seed proteins to identify conglutin β as an allergen, Lup an 1. J. Agric. Food Chem. 2008, 56, 6370-6377.
21. Álvarez-Álvarez, J., Guillamón, E., Crespo, J.-F., Cuadrado, C. et al., Effect of extrusion, boiling, autoclaving and microwave heating on lupine allergenicity. J. Agric. Food Chem. 2005, 53, 1294-1298.
22. Guillamón, E., Burbano, C., Cuadrado, C., Muzquiz, M. M. et al., Effect of an Instantaneous Controlled Pressure Drop on in vitro Allergenicity to Lupins (Lupinus albus var Multolupa). Int. Arch. Allergy Immunol. 2008, 145, 9-14.
23. Blagrove, R.-J., Gillespie, J.-M., Isolation, purification and characterization of the seed globulins of Lupinus angustifolius. Aust. J. Plant Physiol. 1975, 2, 13-27.
24. Laemmli, U.-K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
25. Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 1979, 76, 4350-4354.
26. FAO/WHO: Allergenicity of genetically modified foods. FAO/WHO, Rome 2001.
27. Ramos, P.-C., Ferreira, R.-M., Franco, E., Teixeira, A.-R., Accumulation of a lectin-like breakdown product of beta-conglutin catabolism in cotyledons of germinating Lupinus albus L. seeds. Planta 1997, 203, 26-34.
28. Burks, A.-W., Williams, L.-W., Helm, R.-M., Connaughton, C. et al., Identification of the major peanut allergen, Ara h 1, in patients with atopic dermatitis and positive peanut challenges. J. Allergy Clin. Immunol. 1991, 88, 172-179.
29. Sánchez-Monge, R., Pascual, C.-Y., Diaz-Perales, A., Fernandez-Crespo, J. et al., Isolation and characterization of relevant allergens from boiled lentils. J. Allergy Clin. Immunol. 2000, 106, 955-961.
30. Tsuji, H., Bandon, N., Heimori, M., Purification of characterization of soybean allergen Gly m Bd 28K. Biosci. Biotech. Biochem. 1997, 61, 942-947.
31. Ogawa, T., Samoto, M., Takahashi, K., Soybean allergens and hypoallergenic soybean products. J. Nutr. Sci. Vitamol. 2000, 46, 271-279.
32. Holzhauser, T., Wackermann, O., Ballmer-Weber, B.-K., Bindslev-Jensen, C. et al., Soybean (Glycine max) allergy in Europe: Gly m 5 (β-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy. J. Allergy Clin. Immunol. 2009, 123, 452-458.
33. Wang, F., Robotham, J.-M., Tauber, S.-S., Tawde, P. et al., Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family. J. Allergy Clin. Immunol. 2002, 11, 160-166.
34. Beyer, K., Bardina, L., Grishina, G., Sampson, H.A., Identification of sesame seed allergen by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens. J. Allergy Clin. Immunol. 2002, 110, 154-159.
35. Teuber, S., Jarvis, K.-C., Dandekar, A.-M., Peterson, W.-R. et al., Identification and cloning of a complimentary DNA encoding a vicilin-like proprotein, Jug r 2, from English walnut kernel (Juglans regia), a major food allergen. J. Allergy Clin. Immunol. 1999, 104, 1311-1320.
36. López-Torrejón, G., Salcedo, G., Martín-Esteban, M., Díaz-Perales, A. et al., Len c 1, a mayor allergen and vicilin from lentil seeds: Protein isolation and cDNA cloning. J. Allergy Clin. Immunol. 2003, 112, 1208-1215.
37. Wensing, M., Knulst, A.-C., Persma, S., O'Kane, F. et al., Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1). J. Allergy Clin. Immunol. 2003, 111, 420-424.
38. Sánchez-Monge, R., López-Torrejón, G., Pascual, C.-Y., Varela, J. et al., Vicilin and convicilin are potencial major allergen from pea. Clin. Exp. Allergy 2004, 34, 1747-1753.
39. Manzoni, C., Duranti, M., Eberini, I., Scharnag, H. et al., Subcellular localization of soybean 7S globulin in HepG2 cells and LDL receptor Up-regulation by its α' constituent subunit. J. Nutr. 2003, 133, 2149-2155.
40. Rabjohn, P., Helm, E.-M., Stanley, J.-S., West, C.-M. et al., Molecular cloning and epitope analysis of the peanut allergen Arah 3. J. Clin. Invest. 1999, 103, 535-542.
41. Beardslee, T.-A., Zeece, M.-G., Sarath, G., Markwell, J.-P., Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int. Arch. Allergy Immunol. 2000, 123, 299-307.
42. Barre, A., Jacquet, G., Sordet, C., Culerrier, R. et al., 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. 2007, 44, 3243-3255.
43. Guarneri, F., Guarneri, C., Benvenga, S., Identification of potentially cross-reactive peanut-lupine proteins by computer-assisted search for amino acid sequence homology. Int. Arch. Allergy Immunol. 2005, 138, 273-277.
44. Breiteneder, H., Mills, E.-N. C., Molecular properties of food allergens. J. Allergy Clin. Immunol. 2005, 115, 14-23.
45. Helm, R.-M., Cockrell, G., Connaughton, C., Bannon, G.-A. et al., Soybean G2 glycinin allergen 2. Identification and characterization. Int. Arch. Allergy Immunol. 2000, 123, 213-219.
46. Helm, R.-M., Cockrell, G., Connaughton, C., Sampson, H.-A. et al., A Soybean G2 glycinin allergen 1. Identification and characterization. Int. Arch. Allergy Immunol. 2000, 123, 205-212.
47. Restani, P., Balladio, C., Corsini, E., Fiocchi, A. et al., 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. 2005, 94, 262-266.
48. Sathe, S.-K., Sharma, G.-M., Effects of food processing on food allergens. Mol. Nutr. Food Res. 2009, 53, 970-978.
49. 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.
50. Worm, M., Hompes, S., Fiedler, E.-M., Illner, A.-K. et al., Impact of native, heat-processed and encapsulated hazelnuts on the allergic response in hazelnut-allergic patients. Clin. Exp. Allergy 2009, 39, 159-166