Modeling of allergen proteins found in sea food products

Shellfish are a source of food allergens, and their consumption is the cause of severe allergic reactions in humans. Tropomyosins, a family of muscle proteins, have been identified as the major allergens in shellfish and mollusks species. Nevertheless, few experimentally determined three-dimensional...

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Main Authors: Nataly Galán-Freyle, Jesús Olivero-Verbel, Liney Díaz-López
Format: Article
Language:English
Published: Sociedade Brasileira de Ciência e Tecnologia de Alimentos 2012-06-01
Series:Food Science and Technology
Subjects:
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612012000200028&lng=en&tlng=en
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spelling doaj-79f12a9c7f0848fd8f50e51a0dd773832020-11-25T00:42:36ZengSociedade Brasileira de Ciência e Tecnologia de AlimentosFood Science and Technology1678-457X2012-06-01322393400S0101-20612012000200028Modeling of allergen proteins found in sea food productsNataly Galán-Freyle0Jesús Olivero-Verbel1Liney Díaz-López2University of CartagenaUniversity of CartagenaUniversity of CartagenaShellfish are a source of food allergens, and their consumption is the cause of severe allergic reactions in humans. Tropomyosins, a family of muscle proteins, have been identified as the major allergens in shellfish and mollusks species. Nevertheless, few experimentally determined three-dimensional structures are available in the Protein Data Base (PDB). In this study, 3D models of several homologous of tropomyosins present in marine shellfish and mollusk species (Chaf 1, Met e1, Hom a1, Per v1, and Pen a1) were constructed, validated, and their immunoglobulin E binding epitopes were identified using bioinformatics tools. All protein models for these allergens consisted of long alpha-helices. Chaf 1, Met e1, and Hom a1 had six conserved regions with sequence similarities to known epitopes, whereas Per v1 and Pen a1 contained only one. Lipophilic potentials of identified epitopes revealed a high propensity of hydrophobic amino acids in the immunoglobulin E binding site. This information could be useful to design tropomyosin-specific immunotherapy for sea food allergies.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612012000200028&lng=en&tlng=entropomiosinaIgE reação cruzadaalérgeno
collection DOAJ
language English
format Article
sources DOAJ
author Nataly Galán-Freyle
Jesús Olivero-Verbel
Liney Díaz-López
spellingShingle Nataly Galán-Freyle
Jesús Olivero-Verbel
Liney Díaz-López
Modeling of allergen proteins found in sea food products
Food Science and Technology
tropomiosina
IgE reação cruzada
alérgeno
author_facet Nataly Galán-Freyle
Jesús Olivero-Verbel
Liney Díaz-López
author_sort Nataly Galán-Freyle
title Modeling of allergen proteins found in sea food products
title_short Modeling of allergen proteins found in sea food products
title_full Modeling of allergen proteins found in sea food products
title_fullStr Modeling of allergen proteins found in sea food products
title_full_unstemmed Modeling of allergen proteins found in sea food products
title_sort modeling of allergen proteins found in sea food products
publisher Sociedade Brasileira de Ciência e Tecnologia de Alimentos
series Food Science and Technology
issn 1678-457X
publishDate 2012-06-01
description Shellfish are a source of food allergens, and their consumption is the cause of severe allergic reactions in humans. Tropomyosins, a family of muscle proteins, have been identified as the major allergens in shellfish and mollusks species. Nevertheless, few experimentally determined three-dimensional structures are available in the Protein Data Base (PDB). In this study, 3D models of several homologous of tropomyosins present in marine shellfish and mollusk species (Chaf 1, Met e1, Hom a1, Per v1, and Pen a1) were constructed, validated, and their immunoglobulin E binding epitopes were identified using bioinformatics tools. All protein models for these allergens consisted of long alpha-helices. Chaf 1, Met e1, and Hom a1 had six conserved regions with sequence similarities to known epitopes, whereas Per v1 and Pen a1 contained only one. Lipophilic potentials of identified epitopes revealed a high propensity of hydrophobic amino acids in the immunoglobulin E binding site. This information could be useful to design tropomyosin-specific immunotherapy for sea food allergies.
topic tropomiosina
IgE reação cruzada
alérgeno
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612012000200028&lng=en&tlng=en
work_keys_str_mv AT natalygalanfreyle modelingofallergenproteinsfoundinseafoodproducts
AT jesusoliveroverbel modelingofallergenproteinsfoundinseafoodproducts
AT lineydiazlopez modelingofallergenproteinsfoundinseafoodproducts
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