Structures of CRP antigen-antibody complexes provide insights into the mechanism of specific recognition
Yijian Li1, Qianxi Yu2,3, Mengtan Du2,3
1Department of Laboratory Medicine, Shenzhen Key Laboratory of Medical Laboratory and Molecular Diagnostics, Shenzhen Institute of Translational Medicine, The First Affiliated Hospital of Shenzhen University, Shenzhen Second People's Hospital, Shenzhen, China.
Abstract:
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.
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