Analytical and Bioanalytical Chemistry

, Volume 395, Issue 1, pp 93–102 | Cite as

Maize food allergy: lipid-transfer proteins, endochitinases, and alpha-zein precursor are relevant maize allergens in double-blind placebo-controlled maize-challenge-positive patients

  • Elide A. Pastorello
  • Laura Farioli
  • Valerio Pravettoni
  • Joseph Scibilia
  • Amedeo Conti
  • Donatella Fortunato
  • Linda Borgonovo
  • Simona Bonomi
  • Laura Primavesi
  • Barbara Ballmer-Weber
Original Paper

Abstract

Italian patients with maize anaphylaxis have been shown to have IgE toward two major maize allergens: an alpha-amylase inhibitor and a 9-kDa LTP. A complete study on maize food allergens in patients with positive maize double-blind, placebo-controlled food challenge (DBPCFC) is lacking. The objective was to utilize the three maize protein fractions to identify and characterize the most relevant IgE-binding proteins recognized by the sera of Italian and Swiss patients with either a positive maize-DBPCFC or a history of maize-induced anaphylaxis. Osborne’s protein fractions of maize were extracted to obtain water-soluble, total zein, and total protein fractions. Protein IgE-binding capacity was investigated by SDS-PAGE immunoblotting using the sera from DBPCFC-positive patients and from patients with maize-induced anaphylaxis. Purified maize LTP was used to inhibit the IgE immunoblotting of the three protein fractions. IgE immunoblotting demonstrated that the 9-kDa LTP was recognized by all the Italian patients and by none of the Swiss patients. Other allergens were: 14-kDa α-amylase inhibitor, 30-kDa endochitinases A and -B, 19 kDa zein-β precursor, and 26kDa zein-α precursor; a newly described allergen, the globulin-2 precursor, identified in the total protein fraction. It is noteworthy that maize LTP and endochitinase were cross-reactive with grape LTP and one grape endochitinase. LTP was found to be the only major allergen in Italian patients with either positive maize challenge or a history of maize-induced anaphylaxis. We have identified other maize allergens in subjects with maize food allergy, as grape cross-reactive endochitinase, however, the clinical significance of these proteins needs to be investigated in larger groups of patients with allergy to these food items.

Keywords

Maize allergens Grape allergens Grape cross-reactivity Double-blind placebo-controlled food challenge Maize anaphylaxis Lipid transfer proteins LTP 

References

  1. 1.
    Gonzalo-Garijo MA, Pérez-Calderón R, Muñoz-Rodriguez A, Tormo-Molina R, Silva-Palacios I (2004) Hypersensitivity to maize pollen. Allergy 59(3):365CrossRefGoogle Scholar
  2. 2.
    Weichel M, Glaser AG, Ballmer-Weber BK, Schmid-Grendelmeier P, Crameri R (2006) Wheat and maize thioredoxins: a novel cross-reactive cereal allergen family related to baker's asthma. J Allergy Clin Immunol 117(3):676–681CrossRefGoogle Scholar
  3. 3.
    Cristaudo A, Simonato B, Pasini G, De Rocco M, Curioni A, Giannattasio M (2004) Contact urticaria and protein contact dermatitis from corn in a patient with serum IgE specific for a salt-soluble corn protein of low molecular weight. Contact Dermatitis 51(2):84–87CrossRefGoogle Scholar
  4. 4.
    Scibilia J, Pastorello EA, Zisa G, Ottolenghi A, Ballmer-Weber B, Pravettoni V, Scovena E, Robino A, Ortolani C (2008) Maize food allergy: a double-blind placebo-controlled study. Clin Exp Allergy 38(12):1943–1949CrossRefGoogle Scholar
  5. 5.
    Lian-Chao Li PA, Bedinger C Volk, Jones AD, Cosgrove DJ (2003) Purification and characterization of four beta-expansins (Zea m1 isoforms) from maize pollen. Plant Physiol 132:2073–2085CrossRefGoogle Scholar
  6. 6.
    Petersen A, Dresselhaus T, Grobe K, Becker WM (2006) Protome analysis of maize pollen for allergy relevant components. Proteomics 6:6317–6325CrossRefGoogle Scholar
  7. 7.
    Heiss S, Flicker S, Hamilton DA, Kraft D, Mascarenhans JP, Valenta R (1996) Expression of Zm13, a pollen specific maize protein in Escherichia coli reveals IgE-binding capacity and allergenic potential. FEBS Lett 381(1996):217–221CrossRefGoogle Scholar
  8. 8.
    Pastorello EA, Farioli L, Pravettoni V, Ispano M, Scibola E, Trambaioli C, Giuffrida MG, Ansaloni R, Godovac-Zimmermann J, Conti A, Fortunato D, Ortolani C (2000) The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein. J Allergy Clin Immunol 106(4):744–751CrossRefGoogle Scholar
  9. 9.
    Weichel M, Vergoossen NJ, Bonomi S, Scibilia J, Ortolani C, Ballmer-Weber BK, Pastorello EA, Crameri R (2006) Screening the allergenic repertoires of wheat and maize with sera from double-blind, placebo-controlled food challenge positive patients. Allergy 61(1):128–135Google Scholar
  10. 10.
    Fasoli E, Pastorello EA, Farioli L, Scibilia J, Aldini G, Carini M, Marocco A, Boschetti E, Rigetti PG (2009) Searching for allergens in maize kernels via proteomic tools. J Proteomics 72:501–510CrossRefGoogle Scholar
  11. 11.
    Weichel M, Glaser AG, Ballmer-Weber BK, Schmid-Grendelmeier P, Crameri R (2006) Wheat and maize thioredoxins: a novel cross-reactive cereal allergen family related to baker's asthma. J Allergy Clin Immunol 117(3):676–681CrossRefGoogle Scholar
  12. 12.
    Pasini G, Simonato B, Curioni A, Vincenzi S, Cristaudo A, Santucci B et al (2002) IgE-mediated allergy to corn: 50 kDa protein, belonging to the reduced soluble proteins, is a major allergen. Allergy 57:98–106CrossRefGoogle Scholar
  13. 13.
    Venter C, Skypala I, Dean T (2008) Maize allergy: what we have learned so far. Clin Exp Allergy 38(12):1844–1846CrossRefGoogle Scholar
  14. 14.
    Nakajima O, Teshima R, Takagi K, Okunuki H, Sawada J (2007) ELISA method for monitoring human serum IgE specific for Cry1Ab introduced into genetically modified corn. Regul Toxicol Pharmacol 47:90–95CrossRefGoogle Scholar
  15. 15.
    Pastorello EA, Pompei C, Pravettoni V et al (2003) Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degrees C, as demonstrated in anaphylactic patients and patients with positive double-blind, placebo-controlled food challenge results. J Allergy Clin Immunol 112(4):775–783CrossRefGoogle Scholar
  16. 16.
    Bradford MM (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254CrossRefGoogle Scholar
  17. 17.
    David M, Neville JR (1971) Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system. J Biol Chem 246(20):6328–6334Google Scholar
  18. 18.
    Pastorello EA, Farioli L, Pravettoni V, Ortolani C, Fortunato D, Giuffrida MG, Perono Garoffo L, Calamari AM, Brenna O, Conti A (2003) Identification of grape and wine allergens as an endochitinase 4, a lipid transfer protein, and a thaumatin. J Allergy Clin Immunol 111(2):350–359CrossRefGoogle Scholar
  19. 19.
    Pastorello EA, Farioli L, Conti A, Pravettoni V, Bonomi S, Iametti S, Fortunato D, Scibilia J, Bindslev-Jensen C, Ballmer-Weber B, Robino AM, Ortolani C (2007) Wheat IgE-mediated food allergy in European patients: alpha-amylase inhibitors, lipid transfer proteins and low-molecular-weight glutenins. Allergenic molecules recognized by double-blind, placebo-controlled food challenge. Int Arch Allergy Immunol 144(1):10–22CrossRefGoogle Scholar
  20. 20.
    Pessione E, Giuffrida MG, Prunotto L, Barello C, Mazzoli R, Fortunato D et al (2003) Membrane proteome of Acinetobacter radioresistens S13 during aromatic exposure. Proteomics 3:1070–1076CrossRefGoogle Scholar
  21. 21.
    Hellman U, Wernstedt C, Gonez J, Heldin CH (1995) Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal Biochem 224:451–455CrossRefGoogle Scholar
  22. 22.
    Kader JC (1996) Lipid transfer proteins in plants. Annu Rev Plant Physiol Plant Mol Biol 47:627–654CrossRefGoogle Scholar
  23. 23.
    Sbornik M, Rakoski J, Mempel M, Ollert M, Ring J (2007) IgE mediated type-I-allergy against red wine and grapes. Allergy 62:1339–1348CrossRefGoogle Scholar
  24. 24.
    Zolla L, Rinalducci S, Antonioli P, Righetti PG (2008) Proteomics as a complementary tool for identifying unintended side effects occurring in transgenic maize seeds as a result of genetic modification. J Proteome Res 7(5):1850–1861CrossRefGoogle Scholar

Copyright information

© Springer-Verlag 2009

Authors and Affiliations

  • Elide A. Pastorello
    • 1
  • Laura Farioli
    • 1
  • Valerio Pravettoni
    • 2
  • Joseph Scibilia
    • 1
  • Amedeo Conti
    • 3
  • Donatella Fortunato
    • 3
  • Linda Borgonovo
    • 1
  • Simona Bonomi
    • 2
  • Laura Primavesi
    • 2
  • Barbara Ballmer-Weber
    • 4
  1. 1.Unit of Allergology and Immunology—Niguarda Ca’ Granda HospitalMilanItaly
  2. 2.Allergy Center, Department of Internal Medicine and DermatologyMilanItaly
  3. 3.National Research CouncilTurinItaly
  4. 4.Allergy Center Unit, Department of DermatologyUniversity HospitalZurichSwitzerland

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