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<p>Antigen-antibody specific recognition constitutes fundamental research in molecular drug design and immune diagnostics, where cumulative non-covalent interactions critically determine binding affinities. Current mechanistic understanding of antibody affinity optimization remains incomplete, hindering rational structure-based design of therapeutic antibodies and bispecific variants. This study presents four cryo-EM structures of C-reactive protein (CRP) complexed with heavy-chain antibodies (HCAbs) of varying affinities, resolved at 3.0-3.4 Å resolution. Comparative structural analysis reveals pronounced variations in binding modalities among affinity-differentiated HCAbs, while identifying critical determinants of engagement conformations, providing mechanistic insights for rational optimization of CRP-specific antibodies.</p>

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Structures of CRP antigen-antibody complexes provide insights into the mechanism of specific recognition

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年11月14日

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  • Yijian Li,
  • Qianxi Yu,
  • Mengtan Du,
  • Jian Zhang,
  • Tonggong Liu,
  • Jingzhe Wang,
  • Qingchun Wei,
  • Yong Peng,
  • Chaohui Duan,
  • Dayong Gu,
  • Fuxing Zeng

摘要

Antigen-antibody specific recognition constitutes fundamental research in molecular drug design and immune diagnostics, where cumulative non-covalent interactions critically determine binding affinities. Current mechanistic understanding of antibody affinity optimization remains incomplete, hindering rational structure-based design of therapeutic antibodies and bispecific variants. This study presents four cryo-EM structures of C-reactive protein (CRP) complexed with heavy-chain antibodies (HCAbs) of varying affinities, resolved at 3.0-3.4 Å resolution. Comparative structural analysis reveals pronounced variations in binding modalities among affinity-differentiated HCAbs, while identifying critical determinants of engagement conformations, providing mechanistic insights for rational optimization of CRP-specific antibodies.