Cryo-ET of IgG bivalent binding on SARS-CoV-2 provides structural basis for antibody avidity
Yao, H.; Song, Y.; Huang, Q.; Zhu, M.; Liang, J.; Zhang, Z.; Zhang, X.; Dong, D.; Shi, D.; Wu, Z.; Lu, X.; Wu, H.; Chen, Y.; Li, S.
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The bivalent nature of IgG enhances its neutralization potency against enveloped viruses; however, on-virion structural details of IgG bivalent binding with antigens remain elusive. Here we used cryo-ET to investigate how two potent IgGs P17 and S309 interact with S-trimers on the SARS-CoV-2 surface. We found that these antibodies exploit the mobility of S-trimers to form diverse bivalent binding patterns. P17 stabilizes S-trimers in a one-RBD-up conformation and gathers S-trimer into linear multimers within minutes, whereas S309 primarily forms circular S-trimer assemblies that extend into lattice-like structures. Additionally, both IgGs can facilitate inter-virion coupling through bivalent binding of opposing S-trimers. These findings provide a structural basis for understanding IgG avidity and offer insights for antibody engineering and vaccine design.
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