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Allergenic Lipid Transfer Proteins from Plant-Derived Foods Do Not Immunologically and Clinically Behave Homogeneously: The Kiwifruit LTP as a Model

BACKGROUND: Food allergy is increasingly common worldwide. Tools for allergy diagnosis measuring IgE improved much since allergenic molecules and microarrays started to be used. IgE response toward allergens belonging to the same group of molecules has not been comprehensively explored using such ap...

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Autores principales: Bernardi, Maria Livia, Giangrieco, Ivana, Camardella, Laura, Ferrara, Rosetta, Palazzo, Paola, Panico, Maria Rosaria, Crescenzo, Roberta, Carratore, Vito, Zennaro, Danila, Liso, Marina, Santoro, Mario, Zuzzi, Sara, Tamburrini, Maurizio, Ciardiello, Maria Antonietta, Mari, Adriano
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3219694/
https://www.ncbi.nlm.nih.gov/pubmed/22114713
http://dx.doi.org/10.1371/journal.pone.0027856
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author Bernardi, Maria Livia
Giangrieco, Ivana
Camardella, Laura
Ferrara, Rosetta
Palazzo, Paola
Panico, Maria Rosaria
Crescenzo, Roberta
Carratore, Vito
Zennaro, Danila
Liso, Marina
Santoro, Mario
Zuzzi, Sara
Tamburrini, Maurizio
Ciardiello, Maria Antonietta
Mari, Adriano
author_facet Bernardi, Maria Livia
Giangrieco, Ivana
Camardella, Laura
Ferrara, Rosetta
Palazzo, Paola
Panico, Maria Rosaria
Crescenzo, Roberta
Carratore, Vito
Zennaro, Danila
Liso, Marina
Santoro, Mario
Zuzzi, Sara
Tamburrini, Maurizio
Ciardiello, Maria Antonietta
Mari, Adriano
author_sort Bernardi, Maria Livia
collection PubMed
description BACKGROUND: Food allergy is increasingly common worldwide. Tools for allergy diagnosis measuring IgE improved much since allergenic molecules and microarrays started to be used. IgE response toward allergens belonging to the same group of molecules has not been comprehensively explored using such approach yet. OBJECTIVE: Using the model of lipid transfer proteins (LTPs) from plants as allergens, including two new structures, we sought to define how heterogeneous is the behavior of homologous proteins. METHODS: Two new allergenic LTPs, Act d 10 and Act c 10, have been identified in green (Actinidia deliciosa) and gold (Actinidia chinensis) kiwifruit (KF), respectively, using clinically characterized allergic patients, and their biochemical features comparatively evaluated by means of amino acid sequence alignments. Along with other five LTPs from peach, mulberry, hazelnut, peanut, mugwort, KF LTPs, preliminary tested positive for IgE, have been immobilized on a microarray, used for IgE testing 1,003 allergic subjects. Comparative analysis has been carried out. RESULTS: Alignment of Act d 10 primary structure with the other allergenic LTPs shows amino acid identities to be in a narrow range between 40 and 55%, with a number of substitutions making the sequences quite different from each other. Although peach LTP dominates the IgE immune response in terms of prevalence, epitope recognition driven by sequence heterogeneity has been recorded to be distributed in a wide range of behaviors. KF LTPs IgE positive results were obtained in a patient subset IgE positive for the peach LTP. Anyhow, the negative results on homologous molecules allowed us to reintroduce KF in patients' diet. CONCLUSION: The biochemical nature of allergenic molecule belonging to a group of homologous ones should not be taken as proof of immunological recognition as well. The availability of panels of homologous molecules to be tested using microarrays is valuable to address the therapeutic intervention.
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spelling pubmed-32196942011-11-23 Allergenic Lipid Transfer Proteins from Plant-Derived Foods Do Not Immunologically and Clinically Behave Homogeneously: The Kiwifruit LTP as a Model Bernardi, Maria Livia Giangrieco, Ivana Camardella, Laura Ferrara, Rosetta Palazzo, Paola Panico, Maria Rosaria Crescenzo, Roberta Carratore, Vito Zennaro, Danila Liso, Marina Santoro, Mario Zuzzi, Sara Tamburrini, Maurizio Ciardiello, Maria Antonietta Mari, Adriano PLoS One Research Article BACKGROUND: Food allergy is increasingly common worldwide. Tools for allergy diagnosis measuring IgE improved much since allergenic molecules and microarrays started to be used. IgE response toward allergens belonging to the same group of molecules has not been comprehensively explored using such approach yet. OBJECTIVE: Using the model of lipid transfer proteins (LTPs) from plants as allergens, including two new structures, we sought to define how heterogeneous is the behavior of homologous proteins. METHODS: Two new allergenic LTPs, Act d 10 and Act c 10, have been identified in green (Actinidia deliciosa) and gold (Actinidia chinensis) kiwifruit (KF), respectively, using clinically characterized allergic patients, and their biochemical features comparatively evaluated by means of amino acid sequence alignments. Along with other five LTPs from peach, mulberry, hazelnut, peanut, mugwort, KF LTPs, preliminary tested positive for IgE, have been immobilized on a microarray, used for IgE testing 1,003 allergic subjects. Comparative analysis has been carried out. RESULTS: Alignment of Act d 10 primary structure with the other allergenic LTPs shows amino acid identities to be in a narrow range between 40 and 55%, with a number of substitutions making the sequences quite different from each other. Although peach LTP dominates the IgE immune response in terms of prevalence, epitope recognition driven by sequence heterogeneity has been recorded to be distributed in a wide range of behaviors. KF LTPs IgE positive results were obtained in a patient subset IgE positive for the peach LTP. Anyhow, the negative results on homologous molecules allowed us to reintroduce KF in patients' diet. CONCLUSION: The biochemical nature of allergenic molecule belonging to a group of homologous ones should not be taken as proof of immunological recognition as well. The availability of panels of homologous molecules to be tested using microarrays is valuable to address the therapeutic intervention. Public Library of Science 2011-11-17 /pmc/articles/PMC3219694/ /pubmed/22114713 http://dx.doi.org/10.1371/journal.pone.0027856 Text en Bernardi et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Bernardi, Maria Livia
Giangrieco, Ivana
Camardella, Laura
Ferrara, Rosetta
Palazzo, Paola
Panico, Maria Rosaria
Crescenzo, Roberta
Carratore, Vito
Zennaro, Danila
Liso, Marina
Santoro, Mario
Zuzzi, Sara
Tamburrini, Maurizio
Ciardiello, Maria Antonietta
Mari, Adriano
Allergenic Lipid Transfer Proteins from Plant-Derived Foods Do Not Immunologically and Clinically Behave Homogeneously: The Kiwifruit LTP as a Model
title Allergenic Lipid Transfer Proteins from Plant-Derived Foods Do Not Immunologically and Clinically Behave Homogeneously: The Kiwifruit LTP as a Model
title_full Allergenic Lipid Transfer Proteins from Plant-Derived Foods Do Not Immunologically and Clinically Behave Homogeneously: The Kiwifruit LTP as a Model
title_fullStr Allergenic Lipid Transfer Proteins from Plant-Derived Foods Do Not Immunologically and Clinically Behave Homogeneously: The Kiwifruit LTP as a Model
title_full_unstemmed Allergenic Lipid Transfer Proteins from Plant-Derived Foods Do Not Immunologically and Clinically Behave Homogeneously: The Kiwifruit LTP as a Model
title_short Allergenic Lipid Transfer Proteins from Plant-Derived Foods Do Not Immunologically and Clinically Behave Homogeneously: The Kiwifruit LTP as a Model
title_sort allergenic lipid transfer proteins from plant-derived foods do not immunologically and clinically behave homogeneously: the kiwifruit ltp as a model
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3219694/
https://www.ncbi.nlm.nih.gov/pubmed/22114713
http://dx.doi.org/10.1371/journal.pone.0027856
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