Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel

Abstract Although fish is an important part of the human diet, it is also a common source of food allergy. The major allergen in fish is parvalbumin, a well-conserved Ca2+-binding protein found in the white muscle of many fish species. Here, we studied the solution structure of the parvalbumin Sco j...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Hiroyuki Kumeta, Haruka Nakayama, Kenji Ogura
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
Materias:
R
Q
Acceso en línea:https://doaj.org/article/509fb3e6bfff4ba0852209bf3ff83bf0
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:509fb3e6bfff4ba0852209bf3ff83bf0
record_format dspace
spelling oai:doaj.org-article:509fb3e6bfff4ba0852209bf3ff83bf02021-12-02T15:05:02ZSolution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel10.1038/s41598-017-17281-62045-2322https://doaj.org/article/509fb3e6bfff4ba0852209bf3ff83bf02017-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-17281-6https://doaj.org/toc/2045-2322Abstract Although fish is an important part of the human diet, it is also a common source of food allergy. The major allergen in fish is parvalbumin, a well-conserved Ca2+-binding protein found in the white muscle of many fish species. Here, we studied the solution structure of the parvalbumin Sco j 1, derived from the Pacific mackerel, using nuclear magnetic resonance spectroscopy. We mapped the IgE-binding epitope proposed in a recent study onto the present structure. Interestingly, three of four residues, which were elucidated as key residues of the IgE-binding epitope, were exposed to solvent, whereas one residue faced the inside of the molecule. We expect that this solution structure can be used in future studies attempting to analyze the various IgE-binding modes of these allergens.Hiroyuki KumetaHaruka NakayamaKenji OguraNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Hiroyuki Kumeta
Haruka Nakayama
Kenji Ogura
Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel
description Abstract Although fish is an important part of the human diet, it is also a common source of food allergy. The major allergen in fish is parvalbumin, a well-conserved Ca2+-binding protein found in the white muscle of many fish species. Here, we studied the solution structure of the parvalbumin Sco j 1, derived from the Pacific mackerel, using nuclear magnetic resonance spectroscopy. We mapped the IgE-binding epitope proposed in a recent study onto the present structure. Interestingly, three of four residues, which were elucidated as key residues of the IgE-binding epitope, were exposed to solvent, whereas one residue faced the inside of the molecule. We expect that this solution structure can be used in future studies attempting to analyze the various IgE-binding modes of these allergens.
format article
author Hiroyuki Kumeta
Haruka Nakayama
Kenji Ogura
author_facet Hiroyuki Kumeta
Haruka Nakayama
Kenji Ogura
author_sort Hiroyuki Kumeta
title Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel
title_short Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel
title_full Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel
title_fullStr Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel
title_full_unstemmed Solution structure of the major fish allergen parvalbumin Sco j 1 derived from the Pacific mackerel
title_sort solution structure of the major fish allergen parvalbumin sco j 1 derived from the pacific mackerel
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/509fb3e6bfff4ba0852209bf3ff83bf0
work_keys_str_mv AT hiroyukikumeta solutionstructureofthemajorfishallergenparvalbuminscoj1derivedfromthepacificmackerel
AT harukanakayama solutionstructureofthemajorfishallergenparvalbuminscoj1derivedfromthepacificmackerel
AT kenjiogura solutionstructureofthemajorfishallergenparvalbuminscoj1derivedfromthepacificmackerel
_version_ 1718388954130022400