Clinical Reviews in Allergy & Immunology

, Volume 45, Issue 1, pp 30–46 | Cite as

A Comprehensive Review of Legume Allergy

  • Alok Kumar Verma
  • Sandeep Kumar
  • Mukul Das
  • Premendra D. DwivediEmail author


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.


Legume allergy Hypersensitivity reaction Cross reactivity Allergens 



Thanks are due to SIP-08 of Council of Scientific and industrial Research (CSIR), New Delhi for financial support. Alok Kumar Verma and Sandeep Kumar are thankful to CSIR for the award of their Senior Research Fellowship.

The authors have declared no conflict of interest.

This is CSIR-IITR manuscript # 3025.


  1. 1.
    Kumar S, Verma AK, Das M, Dwivedi PD (2011) Allergenic diversity among plant and animal food proteins. Food Rev Int. doi: 10.1080/87559129.2011.635391
  2. 2.
    Wang J, Sampson HA (2011) Food allergy. J Clin Invest 121(3):827–35PubMedCrossRefGoogle Scholar
  3. 3.
    Waddell L (2011) Living with food allergy. J Fam Health Care 21(4):21–8PubMedGoogle Scholar
  4. 4.
    Ramesh S (2008) Food allergy overview in children. Clin Rev Allergy Immunol 34(2):217–30PubMedCrossRefGoogle Scholar
  5. 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 111:533–40CrossRefGoogle Scholar
  6. 6.
    Skypala I (2011) Adverse food reactions—an emerging issue for adults. J Am Diet Assoc 111(12):1877–91PubMedCrossRefGoogle Scholar
  7. 7.
    Kolacek S (2011) Food hypersensitivity in children. Acta Med Croatica 65(2):155–61PubMedGoogle Scholar
  8. 8.
    Sampson HA (2004) Update on food allergy. J Allergy Clin Immunol 114:127–30CrossRefGoogle Scholar
  9. 9.
    Burks AW, Sampson HA (1999) Anaphylaxis and food allergy. Clin Rev Allergy Immunol 17(3):339–60PubMedCrossRefGoogle Scholar
  10. 10.
    Burks AW, Fuchs RL (1995) Assessment of the endogenous allergens in glyphosate-tolerant and commercial soybean varieties. J Allergy Clin Immunol 96:1008–1010PubMedCrossRefGoogle Scholar
  11. 11.
    Bock SA, Muñoz-Furlong A, Sampson HA (2002) Fatalities due to anaphylactic reactions to foods. J Allergy Clin Immunol 107:191–193CrossRefGoogle Scholar
  12. 12.
    Sampson HA, McCaskill CC (1985) Food hypersensitivity and atopic dermatitis: evaluation of 113 patients. J Pediatr 107:669–675PubMedCrossRefGoogle Scholar
  13. 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 104:452–456PubMedCrossRefGoogle Scholar
  14. 14.
    Sampson HA (2003) Anaphylaxis and emergency treatment. Pediatrics 111:1601PubMedGoogle Scholar
  15. 15.
    Duranti M (2006) Grain legume proteins and nutraceutical properties. Fitoterapia 77:67–82PubMedCrossRefGoogle Scholar
  16. 16.
    Leterme P (2002) Recommendations by health organizations for pulse consumption. Br J Nutr 88:239–242CrossRefGoogle Scholar
  17. 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 147:222–230CrossRefGoogle Scholar
  18. 18.
    Misra A, Prasad R, Das M, Dwivedi PD (2008) Prevalence of legume sensitization in patients with naso-bronchial allergy. Immunopharmacol Immunotoxicol 30:529–42PubMedCrossRefGoogle Scholar
  19. 19.
    Misra A, Prasad R, Das M, Dwivedi PD (2009) Probing novel allergenic proteins of commonly consumed legumes. Immunopharmacol Immunotoxicol 31:186–194PubMedCrossRefGoogle Scholar
  20. 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 58:1144–1151PubMedCrossRefGoogle Scholar
  21. 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 117:29–37PubMedCrossRefGoogle Scholar
  22. 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):1747–53PubMedCrossRefGoogle Scholar
  23. 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):955–61PubMedCrossRefGoogle Scholar
  24. 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 48:2725–2736PubMedCrossRefGoogle Scholar
  25. 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):1157–68PubMedCrossRefGoogle Scholar
  26. 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):104–10PubMedCrossRefGoogle Scholar
  27. 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 44:2868–2879CrossRefGoogle Scholar
  28. 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):24–33PubMedCrossRefGoogle Scholar
  29. 29.
    Gopalan C, Sastri BVR, Balasubramanian SC (1989) Nutritive value of Indian foods. Natinal Institute of Nutrition, Indian Council for Medical Research, HyderabadPubMedCrossRefGoogle Scholar
  30. 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 103:154–158PubMedCrossRefGoogle Scholar
  31. 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 57:362–365PubMedCrossRefGoogle Scholar
  32. 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):883–8CrossRefGoogle Scholar
  33. 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) 35:162–3CrossRefGoogle Scholar
  34. 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 103:233–7PubMedCrossRefGoogle Scholar
  35. 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 41:17–22PubMedGoogle Scholar
  36. 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 64:549–55PubMedCrossRefGoogle Scholar
  37. 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 87:140–145PubMedCrossRefGoogle Scholar
  38. 38.
    Martinez M, Ibanez MD, Fernandez Caldas E (2000) Hypersensitivity to members of the botanical order Fabales (legumes). J Invest Allergol Clin Immunol 10:187–199Google Scholar
  39. 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 6:39–43PubMedCrossRefGoogle Scholar
  40. 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 106:467–71PubMedCrossRefGoogle Scholar
  41. 41.
    Untersmayr E, Jensen Jarolim E (2006) The effect of gastric digestion on food allergy. Curr Opin Allergy Clin Immunol 6:214–9PubMedCrossRefGoogle Scholar
  42. 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 18:984–7PubMedGoogle Scholar
  43. 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 215:405–11PubMedGoogle Scholar
  44. 44.
    Eigenmann PA (2009) Mechanisms of food allergy. Pediatr Allergy Immunol 20:5–11PubMedCrossRefGoogle Scholar
  45. 45.
    Astwood JD, Leach JN, Fuchs RL (1996) Stability of food allergens to digestion in vitro. Nat Biotechnol 14:1269–73PubMedCrossRefGoogle Scholar
  46. 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):461–76PubMedCrossRefGoogle Scholar
  47. 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 39:87–98PubMedCrossRefGoogle Scholar
  48. 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 8:271–285CrossRefGoogle Scholar
  49. 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 93:787–792PubMedCrossRefGoogle Scholar
  50. 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 135:506–512PubMedCrossRefGoogle Scholar
  51. 51.
    Rance F, Dutau G (1997) Practical strategy for the diagnosis of food allergies. Pediatr Pulmonol Suppl 16:228–9PubMedGoogle Scholar
  52. 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):596–600CrossRefGoogle Scholar
  53. 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):174–83PubMedCrossRefGoogle Scholar
  54. 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):30–42PubMedCrossRefGoogle Scholar
  55. 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):471–7Google Scholar
  56. 56.
    Nakanishi K. Berova N, Woody R (1994) Circular dichroism: principles and applications. VCH. p. 473. ISBN 9781560816188Google Scholar
  57. 57.
    Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89(5):392–400PubMedCrossRefGoogle Scholar
  58. 58.
    Greenfield NJ (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1(6):2876–90PubMedCrossRefGoogle Scholar
  59. 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 274:4770–4777PubMedCrossRefGoogle Scholar
  60. 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 169:882–887PubMedGoogle Scholar
  61. 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 395:463–472PubMedCrossRefGoogle Scholar
  62. 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 53:123–131PubMedCrossRefGoogle Scholar
  63. 63.
    Roychaudhuria R, Sarathb G, Zeecec M, Markwell J (2004) Stability of the allergenic soybean Kunitz trypsin inhibitor. Biochim Biophys Acta 1699:207–212Google Scholar
  64. 64.
    Maleki SJ, Hurlburt BK (2004) Structural and functional alterations in major peanut allergens caused by thermal processing. J AOAC Int 87(6):1475–9PubMedGoogle Scholar
  65. 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):1796–804PubMedCrossRefGoogle Scholar
  66. 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):1071–3PubMedCrossRefGoogle Scholar
  67. 67.
    Bannon GA, Ogawa T (2006) Evaluation of available IgE binding epitope data and its utility in bioinformatics. Mol Nutr Food Res 50:638–644PubMedCrossRefGoogle Scholar
  68. 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 134:94–100PubMedCrossRefGoogle Scholar
  69. 69.
    Sampson HA (2001) Utility of food-specific IgE concentrations in predicting symptomatic food allergy. J Allergy Clin Immunol 107:891–6PubMedCrossRefGoogle Scholar
  70. 70.
    Eigenmann PA, Sampson HA (1998) Interpreting skin prick tests in the evaluation of food allergy in children. Pediatr Allergy Immunol 9:186–91PubMedCrossRefGoogle Scholar
  71. 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 30:1540–6PubMedCrossRefGoogle Scholar
  72. 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 42:249–258PubMedGoogle Scholar
  73. 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 113:1129–36PubMedCrossRefGoogle Scholar
  74. 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 51:135–147PubMedCrossRefGoogle Scholar
  75. 75.
    Bohle B, Vieths S (2004) Improving diagnostic tests for food allergy with recombinant allergens. Methods 32:292–299PubMedCrossRefGoogle Scholar
  76. 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 17:350–356PubMedGoogle Scholar
  77. 77.
    Niggemann B, Beyer K (2007) Pitfalls in double-blind, placebo controlled oral food challenges. Allergy 62:729–732PubMedCrossRefGoogle Scholar
  78. 78.
    Sampson HA (1988) Comparative study of commercial food antigen extracts for the diagnosis of food hypersensitivity. J Allergy Clin Immunol 82:718–26PubMedCrossRefGoogle Scholar
  79. 79.
    Sicherer SH (2005) Food protein-induced enterocolitis syndrome: case presentations and management lessons. J Allergy Clin Immunol 115:149–56PubMedCrossRefGoogle Scholar
  80. 80.
    Sampson HA (1999) Food allergy. Part 2: diagnosis and management. J Allergy Clin Immunol 103:981–9PubMedCrossRefGoogle Scholar
  81. 81.
    Beyer K, Teuber SS (2005) Food allergy diagnostics: scientific and unproven procedures. Curr Opin Allergy Clin Immunol 5:261–6PubMedCrossRefGoogle Scholar
  82. 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 107:548–53PubMedCrossRefGoogle Scholar
  83. 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 55:281–5PubMedCrossRefGoogle Scholar
  84. 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 146:177–89PubMedCrossRefGoogle Scholar
  85. 85.
    Stiening H, Szczepanski R, von Mühlendahl KE, Kalveram C (1990) Neurodermatitis and food allergy. Clinical relevance of testing procedures. Monatsschr Kinderheilkd 138:803–7PubMedGoogle Scholar
  86. 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 53:1459–64PubMedCrossRefGoogle Scholar
  87. 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):163–70Google Scholar
  88. 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 119:1197–1202PubMedCrossRefGoogle Scholar
  89. 89.
    Sicherer SH (2002) Clinical update on peanut allergy. Ann Allergy Asthma Immunol 88:350–61PubMedCrossRefGoogle Scholar
  90. 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 260:1450–1452CrossRefGoogle Scholar
  91. 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 109:24–30PubMedCrossRefGoogle Scholar
  92. 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 313:514–7CrossRefGoogle Scholar
  93. 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 88:172–9PubMedCrossRefGoogle Scholar
  94. 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 90:962–9PubMedCrossRefGoogle Scholar
  95. 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):969–78PubMedCrossRefGoogle Scholar
  96. 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 119:265–274PubMedCrossRefGoogle Scholar
  97. 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):295–305CrossRefGoogle Scholar
  98. 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):1422–8PubMedCrossRefGoogle Scholar
  99. 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):1410–7PubMedCrossRefGoogle Scholar
  100. 100.
    International Union of Immunological Societies Allergen Nomenclature: IUIS official list 2007.
  101. 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):20–32PubMedCrossRefGoogle Scholar
  102. 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):88–93PubMedCrossRefGoogle Scholar
  103. 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):143–9PubMedCrossRefGoogle Scholar
  104. 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 106:763–8PubMedCrossRefGoogle Scholar
  105. 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 107:1077–81PubMedCrossRefGoogle Scholar
  106. 106.
    Endres JG (2001) In: Endres JG (ed) Soy protein products—characteristics, nutritional aspects, and utilization. AOCS Publication, Champaign, pp 1–51CrossRefGoogle Scholar
  107. 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 32:1–197Google Scholar
  108. 108.
    Errahali Y, Morisset M, Moneret-Vautrin DA, Kanny G, Metche M, Nicolas JP, Fremont S (2002) Allergen in soy oils. Allergy 57(7):648–649PubMedCrossRefGoogle Scholar
  109. 109.
    Wilson S, Blaschek K, de Mejia E (2005) Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr Rev 63(2):47–58PubMedGoogle Scholar
  110. 110.
    Ogawa A, Samoto M, Takahashi K (2000) Soybean allergens and hypoallergenic soybean products. J Nutr Sci Vitaminol (Tokyo) 46(6):271–9CrossRefGoogle Scholar
  111. 111.
    Renaud C, Cardiet C, Dupont C (1996) Allergy to soy lecithin in a child. J Pediatr Gastroenterol Nutr 22:328–9PubMedCrossRefGoogle Scholar
  112. 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):748–55PubMedCrossRefGoogle Scholar
  113. 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):268–78PubMedCrossRefGoogle Scholar
  114. 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):69–71PubMedCrossRefGoogle Scholar
  115. 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):3114–20PubMedCrossRefGoogle Scholar
  116. 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):555–565PubMedCrossRefGoogle Scholar
  117. 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):1444–1447CrossRefGoogle Scholar
  118. 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):1030–1033PubMedCrossRefGoogle Scholar
  119. 119.
    Shibasaki M, Suzuki S, Tajima S, Nemoto H, Kuroume T (1980) Allergenicity of major component proteins of soybean. Int Arch Allergy Immunol 61:441–448CrossRefGoogle Scholar
  120. 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 56:918–919CrossRefGoogle Scholar
  121. 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 112:1208–15PubMedCrossRefGoogle Scholar
  122. 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):430–8CrossRefGoogle Scholar
  123. 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 53:1462–1468PubMedCrossRefGoogle Scholar
  124. 124.
    Romano C, Ferrara A, Tarallo S (1997) Allergic reaction to lupine seed (Lupinus albus). Allergy 2:113–114Google Scholar
  125. 125.
    Matheu V, De Barrio M, Sierra Z, Gracia-Vara MT, Tornero P, Baeza ML (1999) Lupine-induced anaphylaxis. Ann Allergy Asthma Immunol 83:406–408PubMedCrossRefGoogle Scholar
  126. 126.
    Novembre E, Moriondo M, Bernardini R, Azzari C, Rossi ME, Vierucci A (1999) Lupin allergy in a child. J Allergy Clin Immunol 103:1214–1216PubMedCrossRefGoogle Scholar
  127. 127.
    Kanny G, Guerin L, Moneret-Vautrin DA (2000) Risk of serious asthma due to lupine flour associated with peanut allergy. Rev Med Interne 21:191–194PubMedCrossRefGoogle Scholar
  128. 128.
    Hefle SL, Lemanske RF Jr, Bush RK (1994) Adverse reaction to lupine-fortified pasta. J Allergy Clin Immunol 94:167–172PubMedCrossRefGoogle Scholar
  129. 129.
    Radcliffe M, Scadding G, Brown HM (2005) Lupin flour anaphylaxis. Lancet 365:1360PubMedCrossRefGoogle Scholar
  130. 130.
    Smith WB, Gillis D, Kette FE (2004) Lupin: a new hidden food allergen. Med J Aust 181:219–220PubMedGoogle Scholar
  131. 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 37:108–115PubMedCrossRefGoogle Scholar
  132. 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):6370–6377PubMedCrossRefGoogle Scholar
  133. 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):4567–71PubMedCrossRefGoogle Scholar
  134. 134.
    Ibanez MD, Martinez M, Sanchez JJ, Fernandez-Caldas E (2003) Legume: cross-reactivity. Allergol Immunopathol 31:151–61CrossRefGoogle Scholar
  135. 135.
    Casey R, Domoney C (1999) Pea globulins. In: Shewry PR, Casey R (eds) Seed proteins. Kluwer Academic Publishers, Dordrecht, pp 171–208CrossRefGoogle Scholar
  136. 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 251:717–26PubMedGoogle Scholar
  137. 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 47:185–187PubMedCrossRefGoogle Scholar
  138. 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):1405–9PubMedCrossRefGoogle Scholar
  139. 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):5310–20PubMedCrossRefGoogle Scholar
  140. 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 23:41–3Google Scholar
  141. 141.
    Niphadkar PV, Patil SP, Bapat MM (1992) Legumes the most important food allergen in India. Allergy 47:318CrossRefGoogle Scholar
  142. 142.
    García Ortiz JC, López-Asunsolo A, Cosmes P, Duran AM (1995) Bronchial asthma induced by hypersensitivity to legumes. Allergol Immunopathol (Madr) 23(1):38–40Google Scholar
  143. 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)Google Scholar
  144. 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 94:33–5PubMedCrossRefGoogle Scholar
  145. 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):215–8PubMedCrossRefGoogle Scholar
  146. 146.
    Spiewak R, Dutkiewicz J (2000) Occupational contact dermatitis to Phaseolus vulgaris in a farmer—a case report. Ann Agric Environ Med 7(1):55–9PubMedGoogle Scholar
  147. 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):1561–1568PubMedCrossRefGoogle Scholar
  148. 148.
    Philip J, Prema L (1998) Variability in the anti-nutritional constituents in green gram Vigna radiata. Plant Foods Human Nutrtn 53:99–102CrossRefGoogle Scholar
  149. 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):8–1055CrossRefGoogle Scholar
  150. 150.
    Barnett D, Bonham B, Howden ME (1987) Allergenic cross-reactions among legume foods—an in vitro study. J Allergy Clin Immunol 79(3):433–8PubMedCrossRefGoogle Scholar
  151. 151.
    Huertas AJ, Iriarte P, Polo P, Ayuso R (1995) Urticaria during prick by prick skin test with legumes. Allergy 50S:230Google Scholar
  152. 152.
    European Federation of Asthma and Allergy Associations Food Allergy Brochure EFA Brochure, Box 5, 3830 Leusden, Netherland 1997Google Scholar
  153. 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):499–506PubMedCrossRefGoogle Scholar
  154. 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):299–307PubMedCrossRefGoogle Scholar
  155. 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):565–71PubMedCrossRefGoogle Scholar
  156. 156.
    MoneretVautrin DA (2006) The concept of allergy surveillance: action of the allergy surveillance network. Rev Med Interne 27:S70–2CrossRefGoogle Scholar
  157. 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):273–277PubMedCrossRefGoogle Scholar
  158. 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):251–5PubMedCrossRefGoogle Scholar
  159. 159.
    Pastorello EA, Incorvaia C, Pravettoni V, Ortolani C (1997) Crossreactions in food allergy. Clin Rev Allergy Immunol Winter 15(4):415–27CrossRefGoogle Scholar
  160. 160.
    Weber RW (2001) Cross-reactivity of plant and animal allergens. Clin Rev Allergy Immunol 21(2–3):153–202PubMedCrossRefGoogle Scholar
  161. 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):7154–60PubMedCrossRefGoogle Scholar
  162. 162.
    Sicherer SH, Burks AW, Sampson HA (1998) Clinical features of acute allergic reactions to peanut and tree nuts in children. Pediatrics 102(1):e6PubMedCrossRefGoogle Scholar
  163. 163.
    Ewan PW (1996) Clinical study of peanut and nut allergy in 62 consecutive patients: new features and associations. BMJ 312(7038):1074–8PubMedCrossRefGoogle Scholar
  164. 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):463–471PubMedCrossRefGoogle Scholar
  165. 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 104:991–9PubMedCrossRefGoogle Scholar
  166. 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):263–72PubMedCrossRefGoogle Scholar
  167. 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):517–24PubMedCrossRefGoogle Scholar
  168. 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):366–71Google Scholar

Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  • Alok Kumar Verma
    • 1
  • Sandeep Kumar
    • 1
  • Mukul Das
    • 1
  • Premendra D. Dwivedi
    • 1
    • 2
    Email author
  1. 1.Food, Drug and Chemical Toxicology GroupCSIR-Indian Institute of Toxicology Research, (CSIR-IITR)LucknowIndia
  2. 2.Food, Drug and Chemical Toxicology GroupCSIR-Indian Institute of Toxicology Research (CSIR-IITR)LucknowIndia

Personalised recommendations