×

搜索

搜索
应用案例
Cases
/
/
麻省大学医学院James B Munro 研究团队利用荧光相关光谱技...

麻省大学医学院James B Munro 研究团队利用荧光相关光谱技...

  • 分类:应用案例
  • 发布时间:2022-08-01 16:01
  • 访问量:

【概要描述】Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects cells through binding to angiotensin-converting enzyme 2 (ACE2). This interaction is mediated by the receptor-binding domain (RBD) of the viral spike (S) glycoprotein. Structural and dynamic data have shown that S can adopt multiple conformations, which controls the exposure of the ACE2-binding site in the RBD. Here, using single-molecule Förster resonance energy transfer (smFRET) imaging, we report the effects of ACE2 and antibody binding on the conformational dynamics of S from the Wuhan-1 strain and in the presence of the D614G mutation. We find that D614G modulates the energetics of the RBD position in a manner similar to ACE2 binding. We also find that antibodies that target diverse epitopes, including those distal to the RBD, stabilize the RBD in a position competent for ACE2 binding. Parallel solution-based binding experiments using fluorescence correlation spectroscopy (FCS) indicate antibody-mediated enhancement of ACE2 binding. These findings inform on novel strategies for therapeutic antibody cocktails.

麻省大学医学院James B Munro 研究团队利用荧光相关光谱技...

【概要描述】Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects cells through binding to angiotensin-converting enzyme 2 (ACE2). This interaction is mediated by the receptor-binding domain (RBD) of the viral spike (S) glycoprotein. Structural and dynamic data have shown that S can adopt multiple conformations, which controls the exposure of the ACE2-binding site in the RBD. Here, using single-molecule Förster resonance energy transfer (smFRET) imaging, we report the effects of ACE2 and antibody binding on the conformational dynamics of S from the Wuhan-1 strain and in the presence of the D614G mutation. We find that D614G modulates the energetics of the RBD position in a manner similar to ACE2 binding. We also find that antibodies that target diverse epitopes, including those distal to the RBD, stabilize the RBD in a position competent for ACE2 binding. Parallel solution-based binding experiments using fluorescence correlation spectroscopy (FCS) indicate antibody-mediated enhancement of ACE2 binding. These findings inform on novel strategies for therapeutic antibody cocktails.

  • 分类:应用案例
  • 发布时间:2022-08-01 16:01
  • 访问量:

contact us

联系我们

中科奥辉以创新引领行业,以科技服务社会

联系我们
公司名称:广东中科奥辉科技有限公司
公司电话:0760-8531 9336
邮箱:info@lightedgetech.com
公司地址:广东省中山市翠亨新区翠海道东三围GMP厂房2栋3层

在线留言

留言应用名称:
客户留言
描述:
验证码

版权所有 © 广东中科奥辉科技有限公司        粤ICP备17145470号         网站建设:中企动力      中山

版权所有 © 广东中科奥辉科技有限公司

粤ICP备17145470号

网站建设:中企动力 中山

×
  • info@lightedgetech.com
  • 联系电话: