Tags

Type your tag names separated by a space and hit enter

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.

Abstract

BACKGROUND

In a previous study a 9-kd lipid-transfer protein (LTP) was identified as the major allergen of raw maize in a population of 22 anaphylactic patients. However, the stability of this protein in cooked maize is unknown.

OBJECTIVE

We investigated the allergenicity of 5 maize hybrids and its modification after different thermal treatments by using sera from anaphylactic patients and patients with positive double-blind, placebo-controlled food challenges.

METHODS

Five maize hybrids were extracted by using different methods, obtaining the water-soluble, zein, total zein, glutelin, and total protein fractions. The IgE-binding capacity of the different extracts, both raw and after thermal treatment, was investigated by means of SDS-PAGE immunoblotting. A 9-kd heat-stable allergen was purified by means of HPLC and sequenced. Changes in its secondary structure during and after heating from 25 degrees C to 100 degrees C were monitored by means of circular dichroism.

RESULTS

All raw maize hybrids showed similar protein and IgE-binding profiles. The SDS-PAGE of all the heat-treated hybrids demonstrated a decreased number of stained bands in respect to the raw samples. The IgE immunoblotting demonstrated that the major allergen of the water-soluble, total zein, total protein, and glutelin fractions was a 9-kd protein identified by means of amino acid sequence as an LTP and a sub-tilisin-chymotrypsin inhibitor (in total zein fraction). The IgE-binding capacity of this 9-kd protein remained unchanged after thermal treatments, even though circular dichroism demonstrated an altered secondary structure.

CONCLUSIONS

Maize LTP maintains its IgE-binding capacity after heat treatment, thus being the most eligible candidate for a causative role in severe anaphylactic reactions to both raw and cooked maize.

Links

  • Publisher Full Text
  • Authors+Show Affiliations

    ,

    1st Division of General Medicine Ospedale Maggiore IRCCS, Department of Internal Medicine, University of Milan, Italy.

    , , , , , , , , , ,

    Source

    MeSH

    Adult
    Allergens
    Amino Acid Sequence
    Anaphylaxis
    Antigens, Plant
    Carrier Proteins
    Cooking
    Double-Blind Method
    Electrophoresis, Polyacrylamide Gel
    Female
    Food Hypersensitivity
    Humans
    Immunoblotting
    Immunoglobulin E
    Male
    Mass Spectrometry
    Middle Aged
    Plant Proteins
    Protein Conformation
    Temperature
    Zea mays

    Pub Type(s)

    Clinical Trial
    Journal Article
    Randomized Controlled Trial
    Research Support, Non-U.S. Gov't

    Language

    eng

    PubMed ID

    14564361

    Citation

    Pastorello, Elide A., et al. "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." The Journal of Allergy and Clinical Immunology, vol. 112, no. 4, 2003, pp. 775-83.
    Pastorello EA, Pompei C, Pravettoni V, et al. 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. 2003;112(4):775-83.
    Pastorello, E. A., Pompei, C., Pravettoni, V., Farioli, L., Calamari, A. M., Scibilia, J., ... Ortolani, C. (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. The Journal of Allergy and Clinical Immunology, 112(4), pp. 775-83.
    Pastorello EA, et al. 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. 2003;112(4):775-83. PubMed PMID: 14564361.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - 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. AU - Pastorello,Elide A, AU - Pompei,Carlo, AU - Pravettoni,Valerio, AU - Farioli,Laura, AU - Calamari,Ambra Marianna, AU - Scibilia,Joseph, AU - Robino,Anna Maria, AU - Conti,Amedeo, AU - Iametti,Stefania, AU - Fortunato,Donatella, AU - Bonomi,Simona, AU - Ortolani,Claudio, PY - 2003/10/18/pubmed PY - 2003/11/11/medline PY - 2003/10/18/entrez SP - 775 EP - 83 JF - The Journal of allergy and clinical immunology JO - J. Allergy Clin. Immunol. VL - 112 IS - 4 N2 - BACKGROUND: In a previous study a 9-kd lipid-transfer protein (LTP) was identified as the major allergen of raw maize in a population of 22 anaphylactic patients. However, the stability of this protein in cooked maize is unknown. OBJECTIVE: We investigated the allergenicity of 5 maize hybrids and its modification after different thermal treatments by using sera from anaphylactic patients and patients with positive double-blind, placebo-controlled food challenges. METHODS: Five maize hybrids were extracted by using different methods, obtaining the water-soluble, zein, total zein, glutelin, and total protein fractions. The IgE-binding capacity of the different extracts, both raw and after thermal treatment, was investigated by means of SDS-PAGE immunoblotting. A 9-kd heat-stable allergen was purified by means of HPLC and sequenced. Changes in its secondary structure during and after heating from 25 degrees C to 100 degrees C were monitored by means of circular dichroism. RESULTS: All raw maize hybrids showed similar protein and IgE-binding profiles. The SDS-PAGE of all the heat-treated hybrids demonstrated a decreased number of stained bands in respect to the raw samples. The IgE immunoblotting demonstrated that the major allergen of the water-soluble, total zein, total protein, and glutelin fractions was a 9-kd protein identified by means of amino acid sequence as an LTP and a sub-tilisin-chymotrypsin inhibitor (in total zein fraction). The IgE-binding capacity of this 9-kd protein remained unchanged after thermal treatments, even though circular dichroism demonstrated an altered secondary structure. CONCLUSIONS: Maize LTP maintains its IgE-binding capacity after heat treatment, thus being the most eligible candidate for a causative role in severe anaphylactic reactions to both raw and cooked maize. SN - 0091-6749 UR - https://www.unboundmedicine.com/medline/citation/14564361/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_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0091674903019420 DB - PRIME DP - Unbound Medicine ER -