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热激三龄幼虫的蛋白质组学和生物信息学研究。

Proteomic and Bioinformatic Investigations of Heat-Treated Third-Stage Larvae.

机构信息

Department of Parasitology and Invasive Diseases, National Veterinary Research Institute, Partyzantów Avenue 57, 24-100 Puławy, Poland.

出版信息

Biomolecules. 2020 Jul 16;10(7):1066. doi: 10.3390/biom10071066.

DOI:10.3390/biom10071066
PMID:32708775
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7407331/
Abstract

third-stage larvae are the main source of hidden allergens in marine fish products. Some allergens are thermostable and, even highly processed, could cause hypersensitivity reactions. However, proteome has not been studied under autoclaving conditions of 121 °C for 60 min, which is an important process in the food industry. The aim of the study was the identification and characterization of allergens, potential allergens, and other proteins of heat-treated larvae. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to identify 470 proteins, including allergens-Ani s 1, Ani s 2, Ani s 3, Ani s 4, Ani s 5-and 13 potential allergens that were mainly homologs of spp., spp., and Acari allergens. Ani s 2, Ani s 3, Ani s 5, and three possible allergens were found among the top 25 most abundant proteins. The computational analysis allowed us to detect allergen epitopes, assign protein families, and domains as well as to annotate the localization of proteins. The predicted 3D models of proteins revealed similarities between potential allergens and homologous allergens. Despite the partial degradation of heated antigens, their immunoreactivity with anti- IgG antibodies was confirmed using a Western blot. In conclusion, identified epitopes of allergenic peptides highlighted that the occurrence of proteins in thermally processed fish products could be a potential allergic hazard. Further studies are necessary to confirm the IgE immunoreactivity and thermostability of identified proteins.

摘要

第三期幼虫是海洋鱼类产品中隐藏过敏原的主要来源。一些过敏原具有热稳定性,即使经过高度加工,也可能引起过敏反应。然而,在 121°C 下高压灭菌 60 分钟的条件下,蛋白质组尚未得到研究,这是食品工业中的一个重要过程。本研究的目的是鉴定和表征经热处理的幼虫中的过敏原、潜在过敏原和其他蛋白质。液相色谱-串联质谱 (LC-MS/MS) 用于鉴定 470 种蛋白质,包括过敏原-Ani s 1、Ani s 2、Ani s 3、Ani s 4、Ani s 5 和 13 种潜在过敏原,这些过敏原主要是 spp.、 spp. 和节肢动物过敏原的同源物。在最丰富的前 25 种蛋白质中发现了 Ani s 2、Ani s 3、Ani s 5 和三种可能的过敏原。计算分析允许我们检测过敏原表位、分配蛋白质家族和结构域以及注释蛋白质的定位。蛋白质的预测 3D 模型显示潜在过敏原与同源过敏原之间存在相似性。尽管加热后的 抗原部分降解,但使用 Western blot 证实了它们与抗- IgG 抗体的免疫反应性。总之,鉴定出的过敏原肽表位表明,热加工鱼产品中存在 蛋白质可能是潜在的过敏危害。有必要进一步研究以确认鉴定出的蛋白质的 IgE 免疫反应性和热稳定性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/4af3b49e01c7/biomolecules-10-01066-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/9359001bbc76/biomolecules-10-01066-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/cc15040ce1d3/biomolecules-10-01066-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/e19ab23988af/biomolecules-10-01066-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/fd8c27f0644c/biomolecules-10-01066-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/ed9e6707a8a9/biomolecules-10-01066-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/40e66030f30c/biomolecules-10-01066-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/4af3b49e01c7/biomolecules-10-01066-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/9359001bbc76/biomolecules-10-01066-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/cc15040ce1d3/biomolecules-10-01066-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/e19ab23988af/biomolecules-10-01066-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/fd8c27f0644c/biomolecules-10-01066-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/ed9e6707a8a9/biomolecules-10-01066-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/40e66030f30c/biomolecules-10-01066-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5710/7407331/4af3b49e01c7/biomolecules-10-01066-g007.jpg

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