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Cryo-ET of IgG bivalent binding on SARS-CoV-2 provides structural basis for antibody avidity

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Publicado en:bioRxiv (Mar 2, 2025)
Autor principal: Yao, Hangping
Otros Autores: Song, Yutong, Huang, Qi, Zhu, Miaojin, Liang, Jiaming, Zhang, Zheyuan, Zhang, Xiaodi, Dong, Dongyang, Shi, Danrong, Wu, Zhigang, Lu, Xiangyun, Wu, Haibo, Chen, Yong, Li, Sai
Publicado:
Cold Spring Harbor Laboratory Press
Materias:
Immunoglobulin G
Severe acute respiratory syndrome coronavirus 2
Conformation
Trimers
Avidity
Virions
Acceso en línea:Citation/Abstract
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Resumen: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.Competing Interest StatementThe authors have declared no competing interest.
ISSN:2692-8205
DOI:10.1101/2025.02.28.640788
Fuente:Biological Science Database