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Clinical Reviews in Allergy & Immunology
Erschienen in: Clinical Reviews in Allergy & Immunology 1/2013

01.08.2013

A Comprehensive Review of Legume Allergy

verfasst von: Alok Kumar Verma, Sandeep Kumar, Mukul Das, Premendra D. Dwivedi

Erschienen in: Clinical Reviews in Allergy & Immunology | Ausgabe 1/2013

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Abstract

Legumes belonging to Fabaceae family of the order Fabales are a rich and important source of proteins and many essential elements. Due to its nutritious elements, these are preferably included in human diet in most part of the world. But, unfortunately, IgE binding proteins have been identified in majority of legumes, and allergenic response to these legumes may range from mild skin reactions to life-threatening anaphylactic reaction. Overall, allergenicity due to consumption of legumes in decreasing order may be peanut, soybean, lentil, chickpea, pea, mung bean, and red gram. So far, several allergens from different legumes have been identified and characterized. Most of identified allergens belong to storage proteins family, profilins, or the pathogenesis-related proteins. Legumes also have property of immunological cross-reactivity among themselves and from other sources that also increases the severity of allergenic response to a particular legume. This review summarizes the currently available knowledge on legume allergy and describes the allergenic problems associated with different legumes. It also tries to explore about the legume allergens identified so far by different scientific groups. The culmination of knowledge about identification and characterization of allergens from different legumes will be helpful in diagnosis and treatment of allergy, for development of novel therapeutic strategies, for strict avoidance of particular legume in diet by susceptible individual and also to produce hypoallergenic cultivars of leguminous crop through conventional breeding or genetic modification.
Literatur
1.
2.
3.
Waddell L (2011) Living with food allergy. J Fam Health Care 21(4):21–8PubMed
4.
5.
Von Berg A, Koletzkob S, Grübl A, Filipiak-Pittroff B, Wichmann HE, Bauer CP, Reinhardt D, Berdel D (2003) The effect of hydrolyzed cow's milk formula for allergy prevention in the first year of life: the German Infant Nutritional Intervention Study, a randomized double-blind trial. J Allergy Clin Immunol 111:533–40CrossRef
6.
Skypala I (2011) Adverse food reactions—an emerging issue for adults. J Am Diet Assoc 111(12):1877–91PubMedCrossRef
7.
Kolacek S (2011) Food hypersensitivity in children. Acta Med Croatica 65(2):155–61PubMed
8.
Sampson HA (2004) Update on food allergy. J Allergy Clin Immunol 114:127–30CrossRef
9.
Burks AW, Sampson HA (1999) Anaphylaxis and food allergy. Clin Rev Allergy Immunol 17(3):339–60PubMedCrossRef
10.
Burks AW, Fuchs RL (1995) Assessment of the endogenous allergens in glyphosate-tolerant and commercial soybean varieties. J Allergy Clin Immunol 96:1008–1010PubMedCrossRef
11.
Bock SA, Muñoz-Furlong A, Sampson HA (2002) Fatalities due to anaphylactic reactions to foods. J Allergy Clin Immunol 107:191–193CrossRef
12.
Sampson HA, McCaskill CC (1985) Food hypersensitivity and atopic dermatitis: evaluation of 113 patients. J Pediatr 107:669–675PubMedCrossRef
13.
Yocum MW, Butterfield JH, Klein JS, Volcheck GW, Schroeder DR, Silverstein MD (1999) Epidemiology of anaphylaxis in Olmested County: a population-based study. J Allergy Clin Immunol 104:452–456PubMedCrossRef
14.
Sampson HA (2003) Anaphylaxis and emergency treatment. Pediatrics 111:1601PubMed
15.
16.
Leterme P (2002) Recommendations by health organizations for pulse consumption. Br J Nutr 88:239–242CrossRef
17.
Martinez SIM, Ibanez MD, Fernandez Caldas E, Carnes J (2008) In vitro and in vivo cross-reactivity studies of legume allergy in a Mediterranean population. Int Arch Allergy Immunol 147:222–230CrossRef
18.
Misra A, Prasad R, Das M, Dwivedi PD (2008) Prevalence of legume sensitization in patients with naso-bronchial allergy. Immunopharmacol Immunotoxicol 30:529–42PubMedCrossRef
19.
Misra A, Prasad R, Das M, Dwivedi PD (2009) Probing novel allergenic proteins of commonly consumed legumes. Immunopharmacol Immunotoxicol 31:186–194PubMedCrossRef
20.
Koppelman SJ, Knol EF, Vlooswijk RA, Wensing M, Knulst AC, Hefle SL, Gruppen H, Piersma S (2003) Peanut allergen Ara h 3: isolation from peanuts and biochemical characterization. Allergy 58:1144–1151PubMedCrossRef
21.
Helm R, Cockrell G, Herman E, Burks A, Sampson H, Bannon G (1998) Cellular and molecular characterization of a major soybean allergen. Int Arch Allergy Immunol 117:29–37PubMedCrossRef
22.
Sanchez-Monge R, Lopez-Torrejón G, Pascual CY, Varela J, Martin-Esteban M, Salcedo G (2004) Vicilin and convicilin are potential major allergens from pea. Clin Exp Allergy 34(11):1747–53PubMedCrossRef
23.
Sanchez-Monge R, Pascual CY, Diaz-Perales A, Fernandez-Crespo J, Martin-Esteban M, Salcedo G (2000) Isolation and characterization of relevant allergens from boiled lentils. J Allergy Clin Immunol 106(5):955–61PubMedCrossRef
24.
Misra A, Kumar R, Mishra V, Chaudhari BP, Tripathi A, Das M, Dwivedi PD (2010) Partial characterization of red gram (Cajanus cajan L. Millsp) polypeptides recognized by patients exhibiting rhinitis and bronchial asthma. Food Chem Toxicol 48:2725–2736PubMedCrossRef
25.
Misra A, Kumar R, Mishra V, Chaudhari BP, Raisuddin S, Das M, Dwivedi PD (2011) Potential allergens of green gram (Vigna radiata L. Millsp) identified as members of cupin superfamily and seed albumin. Clin Exp Allergy 41(8):1157–68PubMedCrossRef
26.
Kumari D, Kumar R, Sridhara S, Arora N, Gaur SN, Singh BP (2006) Sensitization to blackgram in patients with bronchial asthma and rhinitis: clinical evaluation and characterization of allergens. Allergy 61(1):104–10PubMedCrossRef
27.
Kumar S, Verma AK, Misra A, Tripathi A, Chaudhari BP, Prasad R, Jain SK, Das M, Dwivedi PD (2011) Allergenic responses of red kidney bean (Phaseolus vulgaris cv chitra) polypeptides in BALB/c mice recognized by bronchial asthma and allergic rhinitis patients. Food Res Int 44:2868–2879CrossRef
28.
Verma AK, Kumar S, Tripathi A, Chaudhari BP, Das M, Dwivedi PD (2012) Chickpea (Cicer arietinum) proteins induce allergic responses in nasobronchial allergic patients and BALB/c mice. Toxicol Lett 210(1):24–33PubMedCrossRef
29.
Gopalan C, Sastri BVR, Balasubramanian SC (1989) Nutritive value of Indian foods. Natinal Institute of Nutrition, Indian Council for Medical Research, HyderabadPubMedCrossRef
30.
Pascual CY, Fernandez-Crespo J, Sanchez-Pastor S, Padial MA, Diaz-Pena JM, Martin-Muñoz F, Martin-Esteban M (1999) Allergy to lentils in Mediterranean pediatric patients. J Allergy Clin Immunol 103:154–158PubMedCrossRef
31.
Dalal I, Binson I, Reifen R, Amitai Z, Shohat T, Rahmani S, Levine A, Ballin A, Somekh E (2002) Food allergy is a matter of geography after all: sesame as a major cause of severe IgE-mediated food allergic reactions among infants and young children in Israel. Allergy 57:362–365PubMedCrossRef
32.
Moneret-Vautrin DA, Guérin L, Kanny G, Flabbee J, Frémont S, Morisset M (1999) Cross-allergenicity of peanut and lupine: the risk of lupine allergy in patients allergic to peanuts. J Allergy Clin Immunol 04(4 Pt 1):883–8CrossRef
33.
Reis AM, Fernandes NP, Marques SL, Paes MJ, Sousa S, Carvalho F, Conde T, Trindade M (2007) Lupine sensitisation in a population of 1,160 subjects. Allergol Immunopathol (Madr) 35:162–3CrossRef
34.
Hieta N, Hasan T, Mäkinen-Kiljunen S, Lammintausta K (2009) Lupin allergy and lupin sensitization among patients with suspected food allergy. Ann Allergy Asthma Immunol 103:233–7PubMedCrossRef
35.
Gayraud J, Mairesse M, Fontaine JF, Thillay A, Leduc V, Rancé F, Parisot L, Moneret-Vautrin DA (2009) The prevalence of sensitization to lupin flour in France and Belgium: a prospective study in 5366 patients, by the allergy vigilance network. Eur Ann Allergy Clin Immunol 41:17–22PubMed
36.
Peeters KA, Koppelman SJ, Penninks AH, Lebens A, Bruijnzeel-Koomen CA, Hefle SL, Taylor SL, van Hoffen E, Knulst AC (2009) Clinical relevance of sensitization to lupine in peanut sensitized adults. Allergy 64:549–55PubMedCrossRef
37.
Patil SP, Niphadkar PV, Bapat MM (2001) Chickpea: a major food allergen in the Indian subcontinent and its clinical and immunochemical correlation. Ann Allergy Asthma Immunol 87:140–145PubMedCrossRef
38.
Martinez M, Ibanez MD, Fernandez Caldas E (2000) Hypersensitivity to members of the botanical order Fabales (legumes). J Invest Allergol Clin Immunol 10:187–199
39.
Crespo JF, Pascual C, Burks AW, Helm RM, Esteban MM (1995) Frequency of food allergy in a pediatric population from Spain. Pediatr Allergy Immunol 6:39–43PubMedCrossRef
40.
Hyman PE, Clarke DD, Everett SL, Sonne B, Stewart D, Harada T, Walsh JH, Taylor IL (1985) Gastric acid secretory function in pre-term infants. J Pediatr 106:467–71PubMedCrossRef
41.
Untersmayr E, Jensen Jarolim E (2006) The effect of gastric digestion on food allergy. Curr Opin Allergy Clin Immunol 6:214–9PubMedCrossRef
42.
Bresson JL, Pang KY, Walker WA (1984) Microvillus membrane differentiation: quantitative difference in cholera toxin binding to the intestinal surface of newborn and adult rabbits. Pediatr Res 18:984–7PubMed
43.
Shub MD, Pang KY, Swann DA, Walker WA (1983) Age related changes in chemical composition and physical properties of mucus glycoproteins from rat small intestine. Biochem J 215:405–11PubMed
44.
45.
Astwood JD, Leach JN, Fuchs RL (1996) Stability of food allergens to digestion in vitro. Nat Biotechnol 14:1269–73PubMedCrossRef
46.
Egger M, Mutschlechner S, Wopfner N, Gadermaier G, Briza P, Ferreira F (2006) Pollen-food syndromes associated with weed pollinosis: an update from the molecular point of view. Allergy 61(4):461–76PubMedCrossRef
47.
Thomas K, Aalbers M, Bannon GA, Bartels M, Dearman RJ, Esdaile DJ, Fu TJ, Glatt CM, Hadfield N, Hatzos C, Hefle SL, Heylings JR, Goodman RE, Henry B, Herouet C, Holsapple M, Ladics GS, Landry TD, MacIntosh SC, Rice EA, Privalle LS, Steiner HY, Teshima R, Van RR, Woolhiser M, Zawodny J (2004) A multi-laboratory evaluation of a common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins. Regul Toxicol Pharmacol 39:87–98PubMedCrossRef
48.
Bannon GA, Goodman RE, Leach JN, Rice E, Fuchs RL, Astwood JD (2002) Digestive stability in the context of assessing the potential allergenicity of food proteins. Comments Toxicol 8:271–285CrossRef
49.
Sorva R, Mäkinen-Kiljunen S, Juntunen-Backman K (1994) B-Lactoglobulin secretion in human milk varies widely after cow's milk ingestion in mothers of infants with cow's milk allergy. J Allergy Clin Immunol 93:787–792PubMedCrossRef
50.
Jarvinen KM, Makinen Kiljunen S, Suomalainen H (1999) Cow's milk challenge through human milk evokes immune responses in infants with cow's milk allergy. J Pediatr 135:506–512PubMedCrossRef
51.
Rance F, Dutau G (1997) Practical strategy for the diagnosis of food allergies. Pediatr Pulmonol Suppl 16:228–9PubMed
52.
Hourihane JO'B, Kilburn SA, Nordlee JA, Hefle SL, Taylor SL, Warner JO (1997) An evaluation of the sensitivity of subjects with peanut allergy to very low doses of peanut protein: a randomized, double-blind, placebo-controlled food challenge study. J Allergy Clin Immunol 100(5):596–600CrossRef
53.
Hiemori M, Ito H, Kimoto M, Yamashita H, Nishizawa K, Maruyama N, Utsumi S, Tsuji H (2004) Identification of the 23-kDa peptide derived from the precursor of gly m bd 28 K, a major soybean allergen, as a new allergen. Biochim Biophys Acta 1675(1–3):174–83PubMedCrossRef
54.
Fötisch K, Altmann F, Haustein D, Vieths S (1999) Involvement of carbohydrate epitopes in the IgE response of celery-allergic patients. Int Arch Allergy Immunol 120(1):30–42PubMedCrossRef
55.
Garcia-Casado G, Sanchez-Monge R, Chrispeels MJ, Armentia A, Salcedo G, Gomez L (1996) Role of complex asparagine-linked glycans in the allergenicity of plant glycoproteins. Glycobiology 1: 6(4):471–7
56.
Nakanishi K. Berova N, Woody R (1994) Circular dichroism: principles and applications. VCH. p. 473. ISBN 9781560816188
57.
Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89(5):392–400PubMedCrossRef
58.
Greenfield NJ (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1(6):2876–90PubMedCrossRef
59.
Koppelman SJ, Bruijnzeel-Koomen CA, Hessing M, de Jongh HH (1999) Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J Biol Chem 274:4770–4777PubMedCrossRef
60.
Sen M, Kopper R, Pons L, Abraham EC, Burks AW, Bannon GA (2002) Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J Immunol 169:882–887PubMed
61.
Lehmann K, Schweimer K, Reese G, Randow S, Suhr M, Becker WM, Vieths S, Rösch P (2006) Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Biochem J 395:463–472PubMedCrossRef
62.
Koppelman SJ, Nieuwenhuizen WF, Gaspari M, Knippels LM, Penninks AH, Knol EF, Hefle SL, de Jongh HH (2005) Reversible denaturation of Brazil nut 2S albumin (Ber e1) and implication of structural destabilization on digestion by pepsin. J Agric Food Chem 53:123–131PubMedCrossRef
63.
Roychaudhuria R, Sarathb G, Zeecec M, Markwell J (2004) Stability of the allergenic soybean Kunitz trypsin inhibitor. Biochim Biophys Acta 1699:207–212
64.
Maleki SJ, Hurlburt BK (2004) Structural and functional alterations in major peanut allergens caused by thermal processing. J AOAC Int 87(6):1475–9PubMed
65.
Jin T, Guo F, Chen YW, Howard A, Zhang YZ (2009) Crystal structure of Ara h 3, a major allergen in peanut. Mol Immunol 46(8–9):1796–804PubMedCrossRef
66.
Cabanos C, Urabe H, Masuda T, Tandang-Silvas MR, Utsumi S, Mikami B, Maruyama N (2010) Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region. Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 9):1071–3PubMedCrossRef
67.
Bannon GA, Ogawa T (2006) Evaluation of available IgE binding epitope data and its utility in bioinformatics. Mol Nutr Food Res 50:638–644PubMedCrossRef
68.
Horsmanheimo L, Harvima IT, Harvima RJ, Ylönen J, Naukkarinen A, Horsmanheimo M (1996) Histamine release in skin monitored with the microdialysis technique does not correlate with the weal size induced by cow allergen. Br J Dermatol 134:94–100PubMedCrossRef
69.
Sampson HA (2001) Utility of food-specific IgE concentrations in predicting symptomatic food allergy. J Allergy Clin Immunol 107:891–6PubMedCrossRef
70.
Eigenmann PA, Sampson HA (1998) Interpreting skin prick tests in the evaluation of food allergy in children. Pediatr Allergy Immunol 9:186–91PubMedCrossRef
71.
Sporik R, Hill DJ, Hosking CS (2000) Specificity of allergen skin testing in predicting positive open food challenges to milk, egg and peanut in children. Clin Exp Allergy 30:1540–6PubMedCrossRef
72.
Aggarwal S, Chhabra SK, Saxena RK, Agarwal MK (2000) Heterogeneity of immune responses to various Aspergillus species in patients with allergic respiratory diseases. Indian J Chest Dis Allied Sci 42:249–258PubMed
73.
Bernstein DI, Wanner M, Borish L, Liss GM (2004) Twelve-year survey of fatal reactions to allergen injections and skin testing: 1990–2001. J Allergy Clin Immunol 113:1129–36PubMedCrossRef
74.
Asero R, Ballmer-Weber BK, Beyer K, Conti A, Dubakiene R, Fernandez-Rivas M, Hoffmann-Sommergruber K, Lidholm J, Mustakov T, Oude Elberink JN, Pumphrey RS, Stahl Skov P, van Ree R, Vlieg-Boerstra BJ, Hiller R, Hourihane JO, Kowalski M, Papadopoulos NG, Wal JM, Mills EN, Vieths S (2007) IgE-mediated food allergy diagnosis: current status and new perspectives. Mol Nutr Food Res 51:135–147PubMedCrossRef
75.
Bohle B, Vieths S (2004) Improving diagnostic tests for food allergy with recombinant allergens. Methods 32:292–299PubMedCrossRef
76.
Gellerstedt M, Bengtsson U, Niggemann B (2007) Methodological issues in the diagnostic work-up of food allergy: a real challenge. J Investig Allergol Clin Immunol 17:350–356PubMed
77.
Niggemann B, Beyer K (2007) Pitfalls in double-blind, placebo controlled oral food challenges. Allergy 62:729–732PubMedCrossRef
78.
Sampson HA (1988) Comparative study of commercial food antigen extracts for the diagnosis of food hypersensitivity. J Allergy Clin Immunol 82:718–26PubMedCrossRef
79.
Sicherer SH (2005) Food protein-induced enterocolitis syndrome: case presentations and management lessons. J Allergy Clin Immunol 115:149–56PubMedCrossRef
80.
Sampson HA (1999) Food allergy. Part 2: diagnosis and management. J Allergy Clin Immunol 103:981–9PubMedCrossRef
81.
Beyer K, Teuber SS (2005) Food allergy diagnostics: scientific and unproven procedures. Curr Opin Allergy Clin Immunol 5:261–6PubMedCrossRef
82.
Roehr CC, Reibel S, Ziegert M, Sommerfeld C, Wahn U, Niggemann B (2001) Atopy patch tests, together with determination of specific IgE levels, reduce the need for oral food challenges in children with atopic dermatitis. J Allergy Clin Immunol 107:548–53PubMedCrossRef
83.
Niggemann B, Reibel S, Wahn U (2000) The atopy patch test (APT)—a useful tool for the diagnosis of food allergy in children with atopic dermatitis. Allergy 55:281–5PubMedCrossRef
84.
de Weck AL, Sanz ML, Gamboa PM, Aberer W, Bienvenu J, Blanca M, Demoly P, Ebo DG, Mayorga L, Monneret G, Sainte-Laudy J (2008) Diagnostic tests based on human basophils: more potentials and perspectives than pitfalls. Int Arch Allergy Immunol 146:177–89PubMedCrossRef
85.
Stiening H, Szczepanski R, von Mühlendahl KE, Kalveram C (1990) Neurodermatitis and food allergy. Clinical relevance of testing procedures. Monatsschr Kinderheilkd 138:803–7PubMed
86.
Atkinson W, Sheldon TA, Shaath N, Whorwell PJ (2004) Food elimination based on IgG antibodies in irritable bowel syndrome: a randomised controlled trial. Gut 53:1459–64PubMedCrossRef
87.
Jenkins JA, Griffiths-Jones S, Shewry PR, Breiteneder H, Mills EN (2005) Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: An in silico analysis. J Allergy Clin Immunol 1:115(1):163–70
88.
Hourihane JO, Aiken R, Briggs R, Gudgeon LA, Grimshaw KE, DunnGalvin A, Roberts SR (2007) The impact of government advice to pregnant mothers regarding peanut avoidance on the prevalence of peanut allergy in United Kingdome children at school entry. J Allergy Clin Immunol 119:1197–1202PubMedCrossRef
89.
90.
Yunginger JW, Sweeney KG, Sturner WQ, Giannandrea LA, Teigland JD, Bray M, Benson PA, York JA, Biedrzycki L, Squillace DL, Helm RM (1988) Fatal food-induced anaphylaxis. J Am Med Assoc 260:1450–1452CrossRef
91.
Taylor SL, Hefle SL, Bindslev-Jensen C, Bock SA, Burks AW, Christie L, Hill DJ, Host A, Hourihane JOB, Lack G, Metcalfe DD, Moneret-Vautrin DA, Vadas PA, Rance F, Skrypec DJ, Trautman TA, Malmheden Yman I, Zeiger RS (2002) Factors affecting the determination of threshold doses for allergenic foods: how much is too much? J Allergy Clin Immunol 109:24–30PubMedCrossRef
92.
Tariq SM, Stevens M, Matthews S, Ridout S, Twiselton R, Hide DW (1996) Cohort study of peanut and tree nut sensitisation by age of 4 years. Br Med J 313:514–7CrossRef
93.
Burks AW, Williams LW, Helm RM, Connaughton C, Cockrell G, O’Brien T (1991) Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. J Allergy Clin Immunol 88:172–9PubMedCrossRef
94.
Burks AW, Williams LW, Connaughton C, Cockrell G, O’Brien TJ, Helm RM (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 challenge. J Allergy Clin Immunol 90:962–9PubMedCrossRef
95.
Eigenmann PA, Burks AW, Bannon GA, Sampson HA (1996) Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies. J Allergy Clin Immunol 98(5 Pt 1):969–78PubMedCrossRef
96.
Kleber-Janke T, Crameri R, Appenzeller U, Schlaak M, Becker WM (1999) Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int Arch Allergy Immunol 119:265–274PubMedCrossRef
97.
Kleber-Janke T, Crameri R, Scheurer S, Vieths S, Becker WM (2001) Patient-tailored cloning of allergens by phage display: peanut (Arachis hypogaea) profilin, a food allergen derived from a rare mRNA. J Chromatogr B: Biomed Sci Appl 756(1–2):295–305CrossRef
98.
Van Wijk F, Hartgring S, Koppelman SJ, Pieters R, Knippels LM (2004) Mixed antibody and T cell responses to peanut and the peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in an oral sensitization model. Clin Exp Allergy 34(9):1422–8PubMedCrossRef
99.
Mittag D, Akkerdaas J, Ballmer-Weber BK, Vogel L, Wensing M, Becker WM, Koppelman SJ, Knulst AC, Helbling A, Hefle SL, Van Ree R, Vieths S (2004) 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(6):1410–7PubMedCrossRef
100.
101.
Asero R, Mistrello G, Roncarolo D, de Vries SC, Gautier MF, Ciurana CL, Verbeek E, Mohammadi T, Knul-Brettlova V, Akkerdaas JH, Bulder I, Aalberse RC, van Ree R (2000) Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion. Int Arch Allergy Immunol 122(1):20–32PubMedCrossRef
102.
Pons L, Chery C, Romano A, Namour F, Artesani MC, Gueant JL (2002) The 18 kDa peanut oleosin is a candidate allergen for IgE-mediated reactions to peanuts. Allergy 57(Suppl 72):88–93PubMedCrossRef
103.
Burks AW, Cockrell G, Connaughton C, Guin J, Allen W, Helm RM (1994) Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. Int Arch Allergy Immunol 105(2):143–9PubMedCrossRef
104.
Maleki SJ, Chung SY, Champagne ET, Raufman JP (2000) The effects of roasting on the allergenic properties of peanut proteins. J Allergy Clin Immunol 106:763–8PubMedCrossRef
105.
Beyer K, Morrow E, Li XM, Bardina L, Bannon GA, Burks AW, Sampson HA (2001) Effects of cooking methods on peanut allergenicity. J Allergy Clin Immunol 107:1077–81PubMedCrossRef
106.
Endres JG (2001) In: Endres JG (ed) Soy protein products—characteristics, nutritional aspects, and utilization. AOCS Publication, Champaign, pp 1–51CrossRef
107.
Becker W, Brasseur D, Bresson JL, Flynn A, Jackson AA, Lagiou P, Mingrone G, Moseley B, Palou A, Przyrembel H, Salminen S, Strobel S, van Loveren H (2004) Opinion of the Scientific Panel on Dietetic Products, Nutrition and Allergies on a request from the Commission relating to the evaluation of allergenic foods for labelling purposes (Request No EFSA-Q-2003-016). EFSA J 32:1–197
108.
Errahali Y, Morisset M, Moneret-Vautrin DA, Kanny G, Metche M, Nicolas JP, Fremont S (2002) Allergen in soy oils. Allergy 57(7):648–649PubMedCrossRef
109.
Wilson S, Blaschek K, de Mejia E (2005) Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr Rev 63(2):47–58PubMed
110.
Ogawa A, Samoto M, Takahashi K (2000) Soybean allergens and hypoallergenic soybean products. J Nutr Sci Vitaminol (Tokyo) 46(6):271–9CrossRef
111.
Renaud C, Cardiet C, Dupont C (1996) Allergy to soy lecithin in a child. J Pediatr Gastroenterol Nutr 22:328–9PubMedCrossRef
112.
Gonzalez R, Polo F, Zapatero L, Caravaca F, Carreira J (1992) Purification and characterization of major inhalant allergens from soybean hulls. Clin Exp Allergy 22(8):748–55PubMedCrossRef
113.
Mittag D, Batori V, Neudecker P, Wiche R, Friis EP, Ballmer-Weber BK, Vieths S, Roggen EL (2006) A novel approach for investigation of specific and cross-reactive IgE epitopes on Bet v 1 and homologous food allergens in individual patients. Mol Immunol 43(3):268–78PubMedCrossRef
114.
Codina R, Lockey RF, Fernandez-Caldas E, Rama R (1999) Identification of the soybean hull allergens responsible for the Barcelona asthma outbreaks. Int Arch Allergy Immunol 119(1):69–71PubMedCrossRef
115.
Natarajan SS, Xu C, Bae H, Caperna TJ, Garrett WM (2006) Characterization of storage proteins in wild (Glycine soja) and cultivated (Glycine max) soybean seeds using proteomic analysis. J Agric Food Chem 54(8):3114–20PubMedCrossRef
116.
Ogawa T, Bando N, Tsuji H, Okajima K, Nishikawa K, Sasaoka K (1991) Investigation of the Ig binding proteins in soybeans by immunoblotting with the sera of the soybean-sensitive patients with atopic dermatitis. J Nutr Sci Vitaminol 37(6):555–565PubMedCrossRef
117.
Yaklich RW, Helm RM, Cockrell G, Herman EM (1999) Analysis of the distribution of the major soybean seed allergens in a core collection of Glycine max accessions. Crop Sci 39(5):1444–1447CrossRef
118.
Ogawa T, Bando N, Tsuji H, Nishikawa K, Kitamura K (1993) Identification of the soybean allergenic protein, Gly m Bd 30 K, with the soybean seed 34-kDa oil-body-associated protein. Biosci Biotechnol Biochem 57(6):1030–1033PubMedCrossRef
119.
Shibasaki M, Suzuki S, Tajima S, Nemoto H, Kuroume T (1980) Allergenicity of major component proteins of soybean. Int Arch Allergy Immunol 61:441–448CrossRef
120.
Crespo JF, Rodrıguez J, Vives R, James JM, Reano M, Daroca P, Burbano C, Muzquiz M (2001) Occupational IgE mediated allergy after exposure to lupine seed flour. J Allergy Clin Immunol 56:918–919CrossRef
121.
Lopez-Torrejon G, Salcedo G, Martin-Esteban M, Diaz-Perales A, Pascual CY, Sanchez-Monge R (2003) Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning. J Allergy Clin Immunol 112:1208–15PubMedCrossRef
122.
Finkina EI, Balandin SV, Serebryakova MV, Potapenko NA, Tagaev AA, Ovchinnikova TV (2007) Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds. Biochemistry (Mosc) 72(4):430–8CrossRef
123.
Cuadrado C, Cabanillas B, Pedrosa MM, Varela A, Guillamón E, Muzquiz M, Crespo JF, Rodriguez J, Burbano C (2009) Influence of thermal processing on IgE reactivity to lentil and chickpea proteins. Mol Nutr Food Res 53:1462–1468PubMedCrossRef
124.
Romano C, Ferrara A, Tarallo S (1997) Allergic reaction to lupine seed (Lupinus albus). Allergy 2:113–114
125.
Matheu V, De Barrio M, Sierra Z, Gracia-Vara MT, Tornero P, Baeza ML (1999) Lupine-induced anaphylaxis. Ann Allergy Asthma Immunol 83:406–408PubMedCrossRef
126.
Novembre E, Moriondo M, Bernardini R, Azzari C, Rossi ME, Vierucci A (1999) Lupin allergy in a child. J Allergy Clin Immunol 103:1214–1216PubMedCrossRef
127.
Kanny G, Guerin L, Moneret-Vautrin DA (2000) Risk of serious asthma due to lupine flour associated with peanut allergy. Rev Med Interne 21:191–194PubMedCrossRef
128.
Hefle SL, Lemanske RF Jr, Bush RK (1994) Adverse reaction to lupine-fortified pasta. J Allergy Clin Immunol 94:167–172PubMedCrossRef
129.
130.
Smith WB, Gillis D, Kette FE (2004) Lupin: a new hidden food allergen. Med J Aust 181:219–220PubMed
131.
Peeters KA, Koppelman SJ, van Hoffen E, van der Tas CWH, den Hartog Jager CF, Penninks AH, Hefle SL, Bruijnzeel-Koomen CA, Knol EF, Knulst AC (2007) Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy? Clin Exp Allergy 37:108–115PubMedCrossRef
132.
Goggin DE, Mir G, Smith WB, Stuckey M, Smith PM (2008) Proteomic analysis of lupin seed proteins to identify conglutin beta as an allergen, Lup an 1. J Agric Food Chem 56(15):6370–6377PubMedCrossRef
133.
Magni C, Herndl A, Sironi E, Scarafoni A, Ballabio C, Restani P, Bernardini R, Novembre E, Vierucci A, Duranti M (2005) One- and two-dimensional electrophoretic identification of IgE-binding polypeptides of Lupinus albus and other legume seeds. J Agric Food Chem 53(11):4567–71PubMedCrossRef
134.
Ibanez MD, Martinez M, Sanchez JJ, Fernandez-Caldas E (2003) Legume: cross-reactivity. Allergol Immunopathol 31:151–61CrossRef
135.
Casey R, Domoney C (1999) Pea globulins. In: Shewry PR, Casey R (eds) Seed proteins. Kluwer Academic Publishers, Dordrecht, pp 171–208CrossRef
136.
Bown D, Ellis TH, Gatehouse JA (1988) The sequence of a gene encoding convicilin from pea (Pisum sativum L) shows that convicilin differs from vicilin by an insertion near the N-terminus. Biochem J 251:717–26PubMed
137.
Martin JA, Compaired JA, de la Hoz B, Quirce S, Alonso MD, Igea JM, Losada E (1992) Bronchial asthma induced by chick pea and lentil. Allergy 47:185–187PubMedCrossRef
138.
Vioque J, Sanchez-Vioque R, Clemente A, Pedroche J, Bautista J, Millan F (1999) Purification and partial characterization of chickpea 2S albumin. J Agric Food Chem 47(4):1405–9PubMedCrossRef
139.
Karamloo F, Wangorsch A, Kasahara H, Davin LB, Haustein D, Lewis NG, Vieths S (2001) Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross-reactive allergens in birch pollen, fruits and vegetables. Eur J Biochem 268(20):5310–20PubMedCrossRef
140.
Pascual CY, Fernandez-Crespo J, Sanchez Pastor S, Ayuso R, Garcia Sanchez G, Martin-Esteban M (2001) Allergy to lentils in Spain. Pediatr Pulmonol Suppl 23:41–3
141.
Niphadkar PV, Patil SP, Bapat MM (1992) Legumes the most important food allergen in India. Allergy 47:318CrossRef
142.
García Ortiz JC, López-Asunsolo A, Cosmes P, Duran AM (1995) Bronchial asthma induced by hypersensitivity to legumes. Allergol Immunopathol (Madr) 23(1):38–40
143.
Kumari D, Arora N, Kasera R, Sridhara S, Kumar R, Singh BP (2012 ) Isolation and characterization of a 28 kDa major allergen from blackgram (Phaseolus mungo). Immunobiology (in press)
144.
Igea JM, Fernandez M, Quirce S, de la Hoz B, Diez Gomez ML (1994) Green bean hypersensitivity: an occupational allergy in a homemaker. J Allergy Clin Immunol 94:33–5PubMedCrossRef
145.
Daroca P, Crespo JF, Reaño M, James JM, Lopez-Rubio A, Rodriguez J (2000) Asthma and rhinitis induced by exposure to raw green beans and chards. Ann Allergy Asthma Immunol 85(3):215–8PubMedCrossRef
146.
Spiewak R, Dutkiewicz J (2000) Occupational contact dermatitis to Phaseolus vulgaris in a farmer—a case report. Ann Agric Environ Med 7(1):55–9PubMed
147.
Zoccatelli G, Pokoj S, Foetisch K, Bartra J, Valero A, San Miguel-Moncin MM, Vieths S, Scheurer S (2010) Identification and characterization of the major allergen of green bean (Phaseolus vulgaris) as a non-specific lipid transfer protein (Pha v 3). Mol Immunol 47(7):1561–1568PubMedCrossRef
148.
Philip J, Prema L (1998) Variability in the anti-nutritional constituents in green gram Vigna radiata. Plant Foods Human Nutrtn 53:99–102CrossRef
149.
Mittag D, Vieths S, Vogel L, Wagner-Loew D, Starke A, Hunziker P, Becker WM, Ballmer-Weber BK (2005) Birch pollen-related food allergy to legumes: identification and characterization of the Bet v 1 homologue in mungbean (Vigna radiata), Vig r 1. Clin Exp Allergy 35(8):8–1055CrossRef
150.
Barnett D, Bonham B, Howden ME (1987) Allergenic cross-reactions among legume foods—an in vitro study. J Allergy Clin Immunol 79(3):433–8PubMedCrossRef
151.
Huertas AJ, Iriarte P, Polo P, Ayuso R (1995) Urticaria during prick by prick skin test with legumes. Allergy 50S:230
152.
European Federation of Asthma and Allergy Associations Food Allergy Brochure EFA Brochure, Box 5, 3830 Leusden, Netherland 1997
153.
Barre A, Borges JP, Rougé P (2005) 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(6):499–506PubMedCrossRef
154.
Beardslee TA, Zeece MG, Sarath G, Markwell JP (2000) Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int Arch Allergy Immunol 123(4):299–307PubMedCrossRef
155.
Viquez OM, Konan KN, Dodo HW (2003) Structure and organization of the genomic clone of a major peanut allergen gene, Ara h 1. Mol Immunol 40(9):565–71PubMedCrossRef
156.
MoneretVautrin DA (2006) The concept of allergy surveillance: action of the allergy surveillance network. Rev Med Interne 27:S70–2CrossRef
157.
Guarneri F, Guarneri C, Benvenga S (2005) Identification of potentially cross-reactive peanut-lupine proteins by computer-assisted search for amino acid sequence homology. Int Arch Allergy Immunol 138(4):273–277PubMedCrossRef
158.
Bush RK, Schroeckenstein D, Meier-Davis S, Balmes J, Rempel D (1988) Soybean flour asthma: detection of allergens by immunoblotting. J Allergy Clin Immunol 82(2):251–5PubMedCrossRef
159.
Pastorello EA, Incorvaia C, Pravettoni V, Ortolani C (1997) Crossreactions in food allergy. Clin Rev Allergy Immunol Winter 15(4):415–27CrossRef
160.
Weber RW (2001) Cross-reactivity of plant and animal allergens. Clin Rev Allergy Immunol 21(2–3):153–202PubMedCrossRef
161.
Fu TJ, Abbott UR, Hatzos C (2002) Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid—a comparative study. J Agric Food Chem 50(24):7154–60PubMedCrossRef
162.
Sicherer SH, Burks AW, Sampson HA (1998) Clinical features of acute allergic reactions to peanut and tree nuts in children. Pediatrics 102(1):e6PubMedCrossRef
163.
Ewan PW (1996) Clinical study of peanut and nut allergy in 62 consecutive patients: new features and associations. BMJ 312(7038):1074–8PubMedCrossRef
164.
de Leon MP, Drew AC, Glaspole IN, Suphioglu C, O'Hehir RE, Rolland JM (2007) IgE cross-reactivity between the major peanut allergen Ara h 2 and tree nut allergens. Mol Immunol 44(4):463–471PubMedCrossRef
165.
Karamloo F, Schmitz N, Scheurer S, Foetisch K, Hoffmann A, Haustein D, Vieths S (1999) Molecular cloning and characterization of a birch pollen minor allergen, Bet v 5, belonging to a family of isoflavone reductase-related proteins. J Allergy Clin Immunol 104:991–9PubMedCrossRef
166.
Vieths S, Frank E, Scheurer S, Meyer HE, Hrazdina G, Haustein D (1998) Characterization of a new IgE-binding 35-kDa protein from birch pollen with cross-reacting homologues in various plant foods. Scand J Immunol 47(3):263–72PubMedCrossRef
167.
Dhyani A, Arora N, Jain VK, Sridhara S, Singh BP (2007) Immunoglobulin E (IgE)-mediated cross-reactivity between mesquite pollen proteins and lima bean, an edible legume. Clin Exp Immunol 149(3):517–24PubMedCrossRef
168.
Branco Ferreira M, Pedro E, Meneses Santos J, Pereira dos Santos MC, Palma Carlos ML, Bartolome B, Palma Carlos AG (2004) Latex and chickpea (Cicer arietinum) allergy: first description of a new association. Allergie et immunologie 36(10):366–71
Metadaten
Titel
A Comprehensive Review of Legume Allergy
verfasst von
Alok Kumar Verma
Sandeep Kumar
Mukul Das
Premendra D. Dwivedi
Publikationsdatum
01.08.2013
Verlag
Springer US
Erschienen in
Clinical Reviews in Allergy & Immunology / Ausgabe 1/2013
Print ISSN: 1080-0549
Elektronische ISSN: 1559-0267
DOI
https://doi.org/10.1007/s12016-012-8310-6

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