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热诱导的腰果过敏原溶解性和IgE结合的改变。

Heat-induced alterations in cashew allergen solubility and IgE binding.

作者信息

Mattison Christopher P, Bren-Mattison Yvette, Vant-Hull Barry, Vargas Aurora M, Wasserman Richard L, Grimm Casey C

机构信息

USDA-Agricultural Research Service, Southern Regional Research Center, New Orleans, LA 70124, USA.

BioMed Bridge, LLC., 3700 Quebec Street Suite #100-230, Denver, CO 80207, USA.

出版信息

Toxicol Rep. 2016 Jan 14;3:244-251. doi: 10.1016/j.toxrep.2015.12.009. eCollection 2016.

DOI:10.1016/j.toxrep.2015.12.009
PMID:28959544
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5615785/
Abstract

Cashew nuts are an increasingly common cause of food allergy. We compare the soluble protein profile of cashew nuts following heating. SDS-PAGE indicate that heating can alter the solubility of cashew nut proteins. The 11S legumin, Ana o 2, dominates the soluble protein content in ready to eat and mildly heated cashew nuts. However, we found that in dark-roasted cashew nuts, the soluble protein profile shifts and the 2S albumin Ana o 3 composes up to 40% of the soluble protein. Analysis of trypsin-treated extracts by LC/MS/MS indicate changes in the relative number and intensity of peptides. The relative cumulative intensity of the 5 most commonly observed Ana o 1 and 2 peptides are altered by heating, while those of the 5 most commonly observed Ana o 3 peptides remaine relatively constant. ELISA experiments indicate that there is a decrease in rabbit IgG and human serum IgE binding to soluble cashew proteins following heating. Our findings indicate that heating can alter the solubility of cashew allergens, resulting in altered IgE binding. Our results support the use of both Ana o 2 and Ana o 3 as potential cashew allergen diagnostic targets.

摘要

腰果是食物过敏日益常见的诱因。我们比较了加热后腰果的可溶性蛋白质谱。十二烷基硫酸钠聚丙烯酰胺凝胶电泳表明加热会改变腰果蛋白质的溶解度。11S豆球蛋白Ana o 2在即食和轻度加热的腰果中占可溶性蛋白质含量的主导地位。然而,我们发现,在深度烘焙的腰果中,可溶性蛋白质谱发生了变化,2S清蛋白Ana o 3占可溶性蛋白质的比例高达40%。通过液相色谱-串联质谱对经胰蛋白酶处理的提取物进行分析,结果表明肽的相对数量和强度发生了变化。加热会改变最常观察到的5种Ana o 1和Ana o 2肽的相对累积强度,而最常观察到的5种Ana o 3肽的相对累积强度则相对保持不变。酶联免疫吸附测定实验表明,加热后兔免疫球蛋白G和人血清免疫球蛋白E与可溶性腰果蛋白的结合减少。我们的研究结果表明,加热会改变腰果过敏原的溶解度,导致免疫球蛋白E结合发生改变。我们的结果支持将Ana o 2和Ana o 3都用作潜在的腰果过敏原诊断靶点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/f5844435241f/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/84585200af50/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/18f7e1e3c3a5/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/4633f015887b/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/e307ecac3ac4/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/f5844435241f/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/84585200af50/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/18f7e1e3c3a5/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/4633f015887b/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/e307ecac3ac4/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb99/5615785/f5844435241f/gr5.jpg

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