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...
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Nature Portfolio
2017
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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) |
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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 |
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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 |