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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):775-83JA

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.

Authors+Show Affiliations

1st Division of General Medicine Ospedale Maggiore IRCCS, Department of Internal Medicine, University of Milan, Italy.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

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 -