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...
Main Authors: | , , |
---|---|
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 |
id |
doaj-79f12a9c7f0848fd8f50e51a0dd77383 |
---|---|
record_format |
Article |
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 |
_version_ |
1725281439594840064 |