• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

通过组合三种抗人α干扰素单克隆抗体提高中和效力

Enhancement of neutralizing efficacy by combining three monoclonal antibodies to human interferon-alpha.

作者信息

Kontsek P, Borecký L, Novák M, Kontseková E, Máciková I

机构信息

Institute of Virology, Slovak Academy of Sciences, Bratislava, Czech.

出版信息

Immunology. 1991 May;73(1):8-11.

PMID:1710604
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1384510/
Abstract

Three murine monoclonal antibodies (mAb) directed to distinct epitopes on recombinant human interferon (IFN)-alpha 1, and three mAb recognizing distinct epitopes on recombinant human interferon (IFN) alpha 1, and three mAb recognizing distinct epitopes on recombinant human IFN-alpha sc, were studied by IFN-neutralizing assays. The efficacy of neutralization of the anti-viral and the anti-proliferative activities of IFN-alpha 1, or IFN-alpha 2c, by the specific antibodies used, individually or in combination, were evaluated. In comparison with single mAb, the mixtures of three mAb against IFN-alpha 1 or three mAb against IFN-alpha 2c were capable of neutralizing more than 10-times larger amounts of IFN-alpha 1 and alpha 2c, respectively. The strong potentiation of the neutralization efficacy resulting from mixing different mAb was demonstrated by neutralization of the anti-viral as well as the anti-proliferative activities of both recombinant IFN. The neutralization experiments support the interpretation that the observed potentiation results from simultaneous interaction of anti-IFN mAb with different epitope specificity.

摘要

通过干扰素中和试验研究了三种针对重组人干扰素(IFN)-α1上不同表位的鼠单克隆抗体(mAb)、三种识别重组人干扰素(IFN)α1上不同表位的mAb以及三种识别重组人IFN-αsc上不同表位的mAb。评估了所使用的特异性抗体单独或联合使用时对IFN-α1或IFN-α2c的抗病毒和抗增殖活性的中和效力。与单克隆mAb相比,三种针对IFN-α1的mAb混合物或三种针对IFN-α2c的mAb混合物分别能够中和比IFN-α1和α2c多10倍以上的量。通过对两种重组干扰素的抗病毒和抗增殖活性进行中和,证明了混合不同mAb导致中和效力的强烈增强。中和实验支持这样的解释,即观察到的增强是由于抗IFN mAb与不同表位特异性同时相互作用所致。

相似文献

1
Enhancement of neutralizing efficacy by combining three monoclonal antibodies to human interferon-alpha.通过组合三种抗人α干扰素单克隆抗体提高中和效力
Immunology. 1991 May;73(1):8-11.
2
Three separate epitopes on human IFN-alpha variants defined by monoclonal antibodies and their role in the binding to receptors.由单克隆抗体定义的人干扰素α变体上的三个独立表位及其在与受体结合中的作用。
Arch Immunol Ther Exp (Warsz). 1992;40(3-4):241-6.
3
Immunochemical characterization of antigenic domains on human interferon-beta: spatially distinct epitopes are associated with both antiviral and antiproliferative activities.人β干扰素抗原结构域的免疫化学特性:空间上不同的表位与抗病毒和抗增殖活性均相关。
Eur J Immunol. 1990 Sep;20(9):1933-9. doi: 10.1002/eji.1830200910.
4
Analysis of antigenic domains on natural and recombinant human IFN-beta by the inhibition of biologic activities with monoclonal antibodies.通过单克隆抗体抑制生物活性分析天然和重组人干扰素-β上的抗原结构域。
J Immunol. 1989 Sep 15;143(6):1887-93.
5
Different functional sites on rIFN-alpha 2 and their relation to the cellular receptor binding site.
J Immunol. 1987 Jan 15;138(2):484-90.
6
Human interferon-gamma has three domains associated with its antiviral function: a neutralizing epitope typing scheme for human interferon-gamma.人干扰素-γ具有与其抗病毒功能相关的三个结构域:人干扰素-γ的一种中和表位分型方案。
Immunology. 1993 May;79(1):131-7.
7
Modification of the antigenic structure of human interferon alpha-2 by PH 2 treatment: a further support for the antigenic relationship between alpha and beta interferons.用pH 2处理对人α-2干扰素抗原结构的修饰:对α和β干扰素之间抗原关系的进一步支持。
Acta Virol. 1990 Apr;34(2):145-54.
8
Epitopes recognized by neutralizing therapy-induced human anti-interferon-alpha antibodies are localized within the N-terminal functional domain of recombinant interferon-alpha 2.
Eur J Immunol. 1996 Sep;26(9):2155-9. doi: 10.1002/eji.1830260929.
9
Cytotoxic T lymphocytes reactive with vesicular stomatitis virus: analysis of specificity with monoclonal antibodies directed to the viral glycoprotein.与水疱性口炎病毒反应的细胞毒性T淋巴细胞:用针对病毒糖蛋白的单克隆抗体分析特异性
J Immunol. 1983 Mar;130(3):1408-12.
10
Production and characterization of four monoclonal antibodies specific for human interferon-alpha-1 and -alpha-2.四种特异性针对人α-1干扰素和α-2干扰素的单克隆抗体的制备与特性鉴定
Biomed Biochim Acta. 1989;48(1):165-76.

引用本文的文献

1
Interferon α kinoid induces neutralizing anti-interferon α antibodies that decrease the expression of interferon-induced and B cell activation associated transcripts: analysis of extended follow-up data from the interferon α kinoid phase I/II study.干扰素α类激动剂诱导中和性抗干扰素α抗体,降低干扰素诱导及B细胞活化相关转录本的表达:干扰素α类激动剂Ⅰ/Ⅱ期研究的长期随访数据分析
Rheumatology (Oxford). 2016 Oct;55(10):1901-5. doi: 10.1093/rheumatology/kew262. Epub 2016 Jun 28.

本文引用的文献

1
The reaction of the anti-interferon-alpha monoclonal antibody, NK2, with different interferons.抗α干扰素单克隆抗体NK2与不同干扰素的反应。
J Gen Virol. 1984 Mar;65 ( Pt 3):629-33. doi: 10.1099/0022-1317-65-3-629.
2
Standardization of the chloramine-T method of protein iodination.蛋白质碘化氯胺-T法的标准化
Proc Soc Exp Biol Med. 1970 Mar;133(3):989-92. doi: 10.3181/00379727-133-34611.
3
The nature of neutralization reaction between effector protein and monoclonal antibody: a quantitative study of neutralization characteristics of anti-interferon antibodies.效应蛋白与单克隆抗体之间中和反应的性质:抗干扰素抗体中和特性的定量研究
Immunology. 1985 Nov;56(3):489-95.
4
Monoclonal antibodies neutralizing human leukocyte acid- and thermolabile interferon alpha.中和人白细胞酸性及热不稳定α干扰素的单克隆抗体
Acta Virol. 1989 May;33(3):254-61.
5
Quantitation of neutralization of interferon by antibody.抗体对干扰素中和作用的定量分析。
Methods Enzymol. 1986;119:558-73. doi: 10.1016/0076-6879(86)19076-8.
6
Neutralization of activity of effector protein by monoclonal antibody: formulation of antibody dose-dependence of neutralization for an equilibrium system of antibody, effector, and its cellular receptor.单克隆抗体对效应蛋白活性的中和作用:针对抗体、效应物及其细胞受体平衡系统的中和抗体剂量依赖性的公式化表述。
Immunology. 1985 Nov;56(3):497-504.