Monoclonal antibodies against the newly identified allergen β-enolase from common carp (Cyprinus carpio)

IF 1.7 3区 农林科学 Q3 CHEMISTRY, APPLIED
Aistė Sližienė, M. Pleckaityte, Mindaugas Zaveckas, K. Juškaitė, Vytautas Rudokas, G. Žvirblis, A. Zvirbliene
{"title":"Monoclonal antibodies against the newly identified allergen β-enolase from common carp (Cyprinus carpio)","authors":"Aistė Sližienė, M. Pleckaityte, Mindaugas Zaveckas, K. Juškaitė, Vytautas Rudokas, G. Žvirblis, A. Zvirbliene","doi":"10.1080/09540105.2022.2028741","DOIUrl":null,"url":null,"abstract":"ABSTRACT β-enolase is a heat-labile fish allergen identified in different fish species. In this study, β-enolase gene was cloned from common carp muscle tissue and the target protein was expressed as a fusion with maltose binding protein (MBP-Eno) in E. coli. Recombinant MBP-Eno was reactive with blood serum specimens of fish-allergic patients, confirming that β-enolase is a newly identified allergen of common carp. Two monoclonal antibodies (MAbs) against recombinant β-enolase were generated that showed cross-reactivity with β-enolases of other organisms. Both antibodies recognized β-enolases from other fish species extracts, while MAb 6E4 showed a broad reactivity with pork, chicken, yeast, and E. coli samples. Epitope mapping using MBP-Eno variants revealed that β-enolase region comprising amino acids 623–698 presumably includes MAb 6E4 epitope. The generated broadly reactive MAb 6E4 directed against a conserved epitope of β-enolases may represent a valuable tool for the characterization of allergen extracts and fish allergy diagnostics.","PeriodicalId":12300,"journal":{"name":"Food and Agricultural Immunology","volume":"33 1","pages":"129 - 149"},"PeriodicalIF":1.7000,"publicationDate":"2022-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food and Agricultural Immunology","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1080/09540105.2022.2028741","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 5

Abstract

ABSTRACT β-enolase is a heat-labile fish allergen identified in different fish species. In this study, β-enolase gene was cloned from common carp muscle tissue and the target protein was expressed as a fusion with maltose binding protein (MBP-Eno) in E. coli. Recombinant MBP-Eno was reactive with blood serum specimens of fish-allergic patients, confirming that β-enolase is a newly identified allergen of common carp. Two monoclonal antibodies (MAbs) against recombinant β-enolase were generated that showed cross-reactivity with β-enolases of other organisms. Both antibodies recognized β-enolases from other fish species extracts, while MAb 6E4 showed a broad reactivity with pork, chicken, yeast, and E. coli samples. Epitope mapping using MBP-Eno variants revealed that β-enolase region comprising amino acids 623–698 presumably includes MAb 6E4 epitope. The generated broadly reactive MAb 6E4 directed against a conserved epitope of β-enolases may represent a valuable tool for the characterization of allergen extracts and fish allergy diagnostics.
鲤鱼过敏原β-烯醇化酶单克隆抗体
摘要β-烯醇化酶是一种在不同鱼类中发现的对热不稳定的鱼类过敏原。本研究从鲤鱼肌肉组织中克隆了β-烯醇化酶基因,并将其与麦芽糖结合蛋白(MBP-Eno)融合表达于大肠杆菌中。重组MBP-Eno与鱼类过敏患者的血清标本反应,证实β-烯醇化酶是一种新发现的常见鲤鱼过敏原。产生了两种针对重组β-烯醇化酶的单克隆抗体(MAbs),它们与其他生物体的β-烯醇酶表现出交叉反应性。两种抗体都能识别其他鱼类提取物中的β-烯醇化酶,而MAb6E4对猪肉、鸡肉、酵母和大肠杆菌样品表现出广泛的反应性。使用MBP-Eno变体的表位定位显示,包含氨基酸623-698的β-烯醇化酶区域可能包括MAb6E4表位。所产生的针对β-烯醇化酶保守表位的广泛反应性MAb6E4可能是表征过敏原提取物和鱼类过敏诊断的有价值的工具。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Food and Agricultural Immunology
Food and Agricultural Immunology 农林科学-毒理学
CiteScore
5.30
自引率
6.70%
发文量
52
审稿时长
2 months
期刊介绍: Food and Agricultural Immunology is an international open access journal publishing original immunological research with applications in food, agricultural, environmental and veterinary science. Submissions describing the use of immunological techniques and methods are particularly welcomed. The journal aims to expand our understanding of the interactions at the interface of food and immune systems including studies on: -Development of diagnostic systems – all types of ligand-based assays, e.g. antibody, aptamer -Application of ligand-based assays for the detection or identification of molecules of interest in food science, agricultural research, veterinary investigations and clinical systems relating to food allergy or sensitivity to agricultural chemicals -Effects of food on the immune system -Studies on allergy and allergic reactions -Investigations into food allergies -Development of allergen-free food systems -Development of novel assay formats -Applications of assay systems to the monitoring of food items in relation to safety and labelling -Food quality issues, e.g. speciation, adulteration and contamination -Comparisons between different analytical techniques The journal publishes research and review articles and is essential reading for food scientists, immunologists and all those concerned with the interaction between food and immune systems.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信