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TitleIgA class switching enhances neutralizing potency against SARS-CoV-2 by increased antibody hinge flexibility.
Journal, issue, pagesAntiviral Res, Vol. 235, Page 106082, Year 2025
Publish dateJan 17, 2025
AuthorsMengxin Xu / Zhaoyong Zhang / Yuzhu Sun / Haoting Mai / Siqi Liu / Shuning Liu / Kexin Lv / Feiyang Yu / Yuanyuan Wang / Xinyu Yue / Jiayi Zhang / Xiaoyu Cai / Ruixin Zhao / Hongjie Lu / Lin Liu / Huanle Luo / Haiyan Zhao / Yanqun Wang / Peng Gong / Shoudeng Chen / Xuping Jing / Jincun Zhao / Yao-Qing Chen /
PubMed AbstractIgA antibodies are critical components of the mucosal immune barrier, providing essential first-line defense against viral infections. In this study, we investigated the impact of antibody class ...IgA antibodies are critical components of the mucosal immune barrier, providing essential first-line defense against viral infections. In this study, we investigated the impact of antibody class switching on neutralization efficacy by engineering recombinant antibodies of different isotypes (IgA1, IgG1) with identical variable regions from SARS-CoV-2 convalescent patients. A potent, broad-spectrum neutralizing monoclonal antibody CAV-C65 exhibited a ten-fold increase in neutralization potency upon switching from IgG1 to IgA1 monomer. Structural analysis revealed that this antibody binds to two adjacent receptor binding domains on the spike protein. Enhanced neutralization by IgA1 was attributed to the combined effects of increased affinity, unique hinge region properties, and potential cross-linking of viral particles. Inhaled CAV-C65 IgA1 demonstrated prophylactic efficacy against lethal SARS-CoV-2 infection in hACE2 mice. These findings highlight the pivotal role of IgA in antiviral immunity and inform the development of IgA-based therapeutics.
External linksAntiviral Res / PubMed:39828085
MethodsEM (single particle)
Resolution3.55 Å
Structure data

61167

9j66

EMDB-61167, PDB-9j66:
Cryo-EM structure of the SARS-CoV-2 S 6P trimer in complex with the human neutralizing antibody Fab fragment CAV-C65 (local refinement)
Method: EM (single particle) / Resolution: 3.55 Å

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / SARS-COV-2 / spike glycoprotein / neutralizing antibody / viral protein-immune system complex (local refinement)

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