{"title":"日本晚疫病中的一种热稳定性过敏原--托品肌苷的鉴定和过敏性分析日本晚疫霉的一种热稳定过敏原","authors":"Meng-Si Li, Fei Xia, Qing-Mei Liu, Jun-Feng Zheng, Tian-Qi Li, Yu-Ni Liao, Gui-Xia Chen, Lian-Zhong Luo, Yi-Xiang Liu, Guang-Ming Liu","doi":"10.1021/acs.jafc.4c10285","DOIUrl":null,"url":null,"abstract":"<i>Lateolabrax japonicus</i>, a prevalent aquatic delicacy, is known to elicit allergic reactions in certain individuals. Nevertheless, the investigation into its allergenic components has remained notably inadequate. In the research, an approximately 35 kDa heat-stable protein of <i>L. japonicus</i> raw/steamed extracts was verified as tropomyosin (TM) by LC–MS/MS. Open reading frame of TM (852 bp) was acquired via PCR amplification, encoding 284 amino acids. The IgE-binding frequency of TM expressed in <i>Escherichia coli</i> was 22.5% among 80 fish-sensitized patients. Furthermore, TM had the ability to activate basophils in 7 patients. In the Balb/c mice model, compared with the PBS group, the levels of specific antibodies (IgE, IgG1, and IgG2a), CD19<sup>+</sup> B cells, IL-4, and IL-10 were significantly increased in the TM group. However, the opposite was indeed the case for CD4<sup>+</sup> TCR-β, CD4<sup>+</sup> CD25<sup>+</sup> Fox p 3<sup>+</sup> cells, and IFN-γ. These findings regarding an allergen assist in conducting component-resolved diagnoses and therapeutic research for fish allergy.","PeriodicalId":41,"journal":{"name":"Journal of Agricultural and Food Chemistry","volume":"114 1","pages":""},"PeriodicalIF":5.7000,"publicationDate":"2024-12-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Identification and Allergenicity Analysis of Tropomyosin: A Heat-Stable Allergen in Lateolabrax japonicus\",\"authors\":\"Meng-Si Li, Fei Xia, Qing-Mei Liu, Jun-Feng Zheng, Tian-Qi Li, Yu-Ni Liao, Gui-Xia Chen, Lian-Zhong Luo, Yi-Xiang Liu, Guang-Ming Liu\",\"doi\":\"10.1021/acs.jafc.4c10285\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<i>Lateolabrax japonicus</i>, a prevalent aquatic delicacy, is known to elicit allergic reactions in certain individuals. Nevertheless, the investigation into its allergenic components has remained notably inadequate. In the research, an approximately 35 kDa heat-stable protein of <i>L. japonicus</i> raw/steamed extracts was verified as tropomyosin (TM) by LC–MS/MS. Open reading frame of TM (852 bp) was acquired via PCR amplification, encoding 284 amino acids. The IgE-binding frequency of TM expressed in <i>Escherichia coli</i> was 22.5% among 80 fish-sensitized patients. Furthermore, TM had the ability to activate basophils in 7 patients. In the Balb/c mice model, compared with the PBS group, the levels of specific antibodies (IgE, IgG1, and IgG2a), CD19<sup>+</sup> B cells, IL-4, and IL-10 were significantly increased in the TM group. However, the opposite was indeed the case for CD4<sup>+</sup> TCR-β, CD4<sup>+</sup> CD25<sup>+</sup> Fox p 3<sup>+</sup> cells, and IFN-γ. These findings regarding an allergen assist in conducting component-resolved diagnoses and therapeutic research for fish allergy.\",\"PeriodicalId\":41,\"journal\":{\"name\":\"Journal of Agricultural and Food Chemistry\",\"volume\":\"114 1\",\"pages\":\"\"},\"PeriodicalIF\":5.7000,\"publicationDate\":\"2024-12-18\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Agricultural and Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1021/acs.jafc.4c10285\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"AGRICULTURE, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Agricultural and Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1021/acs.jafc.4c10285","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
Identification and Allergenicity Analysis of Tropomyosin: A Heat-Stable Allergen in Lateolabrax japonicus
Lateolabrax japonicus, a prevalent aquatic delicacy, is known to elicit allergic reactions in certain individuals. Nevertheless, the investigation into its allergenic components has remained notably inadequate. In the research, an approximately 35 kDa heat-stable protein of L. japonicus raw/steamed extracts was verified as tropomyosin (TM) by LC–MS/MS. Open reading frame of TM (852 bp) was acquired via PCR amplification, encoding 284 amino acids. The IgE-binding frequency of TM expressed in Escherichia coli was 22.5% among 80 fish-sensitized patients. Furthermore, TM had the ability to activate basophils in 7 patients. In the Balb/c mice model, compared with the PBS group, the levels of specific antibodies (IgE, IgG1, and IgG2a), CD19+ B cells, IL-4, and IL-10 were significantly increased in the TM group. However, the opposite was indeed the case for CD4+ TCR-β, CD4+ CD25+ Fox p 3+ cells, and IFN-γ. These findings regarding an allergen assist in conducting component-resolved diagnoses and therapeutic research for fish allergy.
期刊介绍:
The Journal of Agricultural and Food Chemistry publishes high-quality, cutting edge original research representing complete studies and research advances dealing with the chemistry and biochemistry of agriculture and food. The Journal also encourages papers with chemistry and/or biochemistry as a major component combined with biological/sensory/nutritional/toxicological evaluation related to agriculture and/or food.