Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degree C, as demonstrated in anaphylactic patients and patients with double-blind, placebo-controlled food challenge results. (Articolo in rivista)

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  • Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degree C, as demonstrated in anaphylactic patients and patients with double-blind, placebo-controlled food challenge results. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Pastorello E.A.1, Pompei C.2, Pravettoni V.1, Farioli L.3, Calamari AM.1, Scibilia J.4, Robino AM.1, Conti A.5, Iametti S.6, Fortunato D.5, Bonomi S.1, Ortolani C.4 (2003)
    Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degree C, as demonstrated in anaphylactic patients and patients with double-blind, placebo-controlled food challenge results.
    in Journal of allergy and clinical immunology
    (literal)
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  • Pastorello E.A.1, Pompei C.2, Pravettoni V.1, Farioli L.3, Calamari AM.1, Scibilia J.4, Robino AM.1, Conti A.5, Iametti S.6, Fortunato D.5, Bonomi S.1, Ortolani C.4 (literal)
Pagina inizio
  • 775 (literal)
Pagina fine
  • 783 (literal)
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  • Questa pubblicazione è stata realizzata nell'ambito del progetto CE QLK4 2001-00301, titolo “Food Allergy Risk Evaluation based on improved Diagnosis, Allergens and test methods” (FAREDAT), 2002-2004. Impact Factor 5.506 (literal)
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  • 112 (literal)
Rivista
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  • Un moderno approccio allo studio delle allergie alimentari deve prendere in considerazione le possibili modificazioni a cui vanno incontro le proteine allergeniche - cioè quelle proteine che si legano alle IgE dei soggetti allergici - in seguito ai normali processi di cottura. Ad esempio la tostatura delle noccioline americane (peanuts) ne aumenta notevolmente l'allergenicità; per contro è noto che l'allergenicità di alimenti contenenti enzimi della classe delle chitinasi viene completamente abolita dal riscaldamento. In questo lavoro, viene per la prima volta dimostrato che il maggiore allergene del mais è una Lipid Transfer Protein (LTP) e che questa proteina, essendo termoresistente, mantiene il suo potenziale allergenico anche dopo prolungata cottura potendo provocare anche severe reazioni anafilattiche. (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • 1 Allergy Centre, Ospedale Maggiore IRCCS, Milano; 2 Dep. Foof Science and Microbiology, Università di Milano; 3 UOOOML, CEMOC, I.C.P., Milano; 4 Bizzozzero Division, Niguarda Hospital, Milano; 5 CNR-ISPA, Torino; 6 Dep. Agri-Food Molecular Sciences, Università di Milano. (literal)
Titolo
  • Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degree C, as demonstrated in anaphylactic patients and patients with double-blind, placebo-controlled food challenge results. (literal)
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. (literal)
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