文献知网节
  • 记笔记

Antibody Associated Virus to Potential Epitopes:A Reverse Epitope Mapping Strategy

Liam J.FanningAmruta S.NaikOrla CrosbieElizabeth Kenny-Walsh

University College Cork Ireland

摘要:Background:Neutralising antibodies(nAbs) are produced in response to HCV infection by the humoral immune system.The current study explores potential epitopes in the E2 glycoprotein of antibody associated HCV using a chemically linked peptides on scaffolds(CLIPS) technology.Methodology:Amino acid region located within 384-619 in the E2 glycoprotein was to generate linear peptides,loop mimics and helical structural peptide library.A PEPSCAN-based ELISA was used to assess the peptide binding characteristic of several HCV-Fab like molecules(HCV-Fab).The in vitro pseudoparticle neutralisation potential of the HCV-Fabs was accessed.Results:The epitope mapping analysis identified five potential binding motifs in the E2 glycoprotein,i.e.,Epitope AN1393-405 located within the immunodominant HVR1 domain,AN2433-445 overlaped AN3428-447 which share amino acid residues with the monoclonal antibody epitope AR3 C,AN4539-551 epitope is located within the conformationally flexible Ig like domain of the E2 glycoprotein and AN5599-608 was positioned at an inter-genotypic variable region(IgVR 570-580).The role of AN4 and AN5 in HCV infectivity and neutralisation requires further investigation.Using a virus capture methodology the monocolonal antibody AP33 was only partially able to capture known epitope positive serum derived virus.Significantly,this suggests that not all epitopes are equally accessible.In conclusion:Our data indicates that patient derived HCV-Fab target multiple epitopes.Combination of HCV-Fabs resulted in a greater reduction in the infectivity of HCVpp as compared to the individual Fabs.Whether the inability to capture epitope positive virus is due to the lipoviral nature of HCV remains to be determined.
会议名称:

BIT’s 10th World Congress of Vaccine Singapore-2017

会议时间:

2017-11-15

会议地点:

Singapore

  • 专辑:

    医药卫生科技

  • 专题:

    基础医学

  • 分类号:

    R392

  • 手机阅读
    即刻使用手机阅读
    第一步

    扫描二维码下载

    "移动知网-全球学术快报"客户端

    第二步

    打开“全球学术快报”

    点击首页左上角的扫描图标

    第三步

    扫描二维码

    手机同步阅读本篇文献

  • CAJ下载
  • PDF下载

下载手机APP用APP扫此码同步阅读该篇文章

下载:1 页码:66 页数:1 大小:102k

相关推荐
  • 相似文献
  • 读者推荐
  • 相关基金文献
  • 关联作者
  • 相关视频