Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas
Abstract BACKGROUND Molluscan shellfish, including oysters, often cause allergic reactions in sensitive people throughout the world. It has been demonstrated that arginine kinase (AK) is one of the major allergens of oyster. The present study aimed to evaluate the immunoreactivity and structure of o...
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crwiley:10.1002/jsfa.11691 2024-05-19T07:39:20+00:00 Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas Zhao, Xiaohan Li, Guoming Feng, Xiaowen Cheng, Qingli Lu, Zhihao Gu, Ruizeng Lu, Jun Liu, Wenying 2021 http://dx.doi.org/10.1002/jsfa.11691 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.11691 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/jsfa.11691 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Journal of the Science of Food and Agriculture volume 102, issue 8, page 3435-3445 ISSN 0022-5142 1097-0010 Nutrition and Dietetics Agronomy and Crop Science Food Science Biotechnology journal-article 2021 crwiley https://doi.org/10.1002/jsfa.11691 2024-04-22T07:32:34Z Abstract BACKGROUND Molluscan shellfish, including oysters, often cause allergic reactions in sensitive people throughout the world. It has been demonstrated that arginine kinase (AK) is one of the major allergens of oyster. The present study aimed to evaluate the immunoreactivity and structure of oyster AK as affected by heat treatment, pH change, and in vitro digestion. What is more, the immunoglobulin E‐binding epitopes of this allergen were also predicted and validated. RESULTS Thermal and pH assays revealed that AK was unstable at temperature >40 °C or pH ≤5.0 by sodium dodecyl sulfate polyacrylamide gel electrophoresis and circular dichroism, and the digestibility assays suggested that AK was more easily digested by pepsin than by trypsin and chymotrypsin. The potential epitopes were predicted through immunoinformatics tools, and seven linear epitopes were identified by indirect competition enzyme‐linked immunosorbent assay with pooled sera and individual serum from oyster‐allergic patients. The critical amino acids in each epitope were also confirmed using mutant peptides. These linear epitopes and critical amino acids were apt to distribute on the outer surface of homology‐based AK model. Moreover, the three denaturants (sodium dodecyl sulfate, β ‐mercaptoethanol, and urea) can destroy the spatial structure of AK and increase or reduce its allergenicity by denaturation treatments. CONCLUSION Processing conditions lay the foundation for the variation of allergenicity. Seven linear epitopes and their critical amino acids were identified by indirect competitive enzyme‐linked immunosorbent assay. These findings will be helpful in allergy diagnosis and development of hypoallergenic products in the near future. © 2021 Society of Chemical Industry. Article in Journal/Newspaper Crassostrea gigas Wiley Online Library Journal of the Science of Food and Agriculture |
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Open Polar |
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Wiley Online Library |
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crwiley |
language |
English |
topic |
Nutrition and Dietetics Agronomy and Crop Science Food Science Biotechnology |
spellingShingle |
Nutrition and Dietetics Agronomy and Crop Science Food Science Biotechnology Zhao, Xiaohan Li, Guoming Feng, Xiaowen Cheng, Qingli Lu, Zhihao Gu, Ruizeng Lu, Jun Liu, Wenying Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas |
topic_facet |
Nutrition and Dietetics Agronomy and Crop Science Food Science Biotechnology |
description |
Abstract BACKGROUND Molluscan shellfish, including oysters, often cause allergic reactions in sensitive people throughout the world. It has been demonstrated that arginine kinase (AK) is one of the major allergens of oyster. The present study aimed to evaluate the immunoreactivity and structure of oyster AK as affected by heat treatment, pH change, and in vitro digestion. What is more, the immunoglobulin E‐binding epitopes of this allergen were also predicted and validated. RESULTS Thermal and pH assays revealed that AK was unstable at temperature >40 °C or pH ≤5.0 by sodium dodecyl sulfate polyacrylamide gel electrophoresis and circular dichroism, and the digestibility assays suggested that AK was more easily digested by pepsin than by trypsin and chymotrypsin. The potential epitopes were predicted through immunoinformatics tools, and seven linear epitopes were identified by indirect competition enzyme‐linked immunosorbent assay with pooled sera and individual serum from oyster‐allergic patients. The critical amino acids in each epitope were also confirmed using mutant peptides. These linear epitopes and critical amino acids were apt to distribute on the outer surface of homology‐based AK model. Moreover, the three denaturants (sodium dodecyl sulfate, β ‐mercaptoethanol, and urea) can destroy the spatial structure of AK and increase or reduce its allergenicity by denaturation treatments. CONCLUSION Processing conditions lay the foundation for the variation of allergenicity. Seven linear epitopes and their critical amino acids were identified by indirect competitive enzyme‐linked immunosorbent assay. These findings will be helpful in allergy diagnosis and development of hypoallergenic products in the near future. © 2021 Society of Chemical Industry. |
format |
Article in Journal/Newspaper |
author |
Zhao, Xiaohan Li, Guoming Feng, Xiaowen Cheng, Qingli Lu, Zhihao Gu, Ruizeng Lu, Jun Liu, Wenying |
author_facet |
Zhao, Xiaohan Li, Guoming Feng, Xiaowen Cheng, Qingli Lu, Zhihao Gu, Ruizeng Lu, Jun Liu, Wenying |
author_sort |
Zhao, Xiaohan |
title |
Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas |
title_short |
Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas |
title_full |
Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas |
title_fullStr |
Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas |
title_full_unstemmed |
Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas |
title_sort |
physicochemical characterization and linear epitopes identification of arginine kinase allergen from crassostrea gigas |
publisher |
Wiley |
publishDate |
2021 |
url |
http://dx.doi.org/10.1002/jsfa.11691 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jsfa.11691 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/jsfa.11691 |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_source |
Journal of the Science of Food and Agriculture volume 102, issue 8, page 3435-3445 ISSN 0022-5142 1097-0010 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/jsfa.11691 |
container_title |
Journal of the Science of Food and Agriculture |
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1799478900285243392 |