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TitleBroadly Sarbecovirus-Neutralizing Antibodies Induced by Ancestral SARS-CoV-2 Infection.
Journal, issue, pagesViruses, Vol. 17, Issue 10, Year 2025
Publish dateSep 23, 2025
AuthorsYiwei Zhang / Zhen Zhang / Feiyang Yu / Xianying Chen / Shangyu Yang / Jingyi Lin / Genmao Liu / Xinyang Liu / Ming Guo / Yu Chen / Ke Lan / Haiyan Zhao /
PubMed AbstractThe COVID-19 pandemic, driven by SARS-CoV-2, continues to challenge global health due to emerging variants and the potential risk posed by related sarbecoviruses. Neutralizing antibodies targeting ...The COVID-19 pandemic, driven by SARS-CoV-2, continues to challenge global health due to emerging variants and the potential risk posed by related sarbecoviruses. Neutralizing antibodies targeting the spike (S) glycoprotein, particularly the receptor-binding domain (RBD), play a crucial role in viral neutralization and vaccine design. Although broadly neutralizing anti-RBD antibodies have been identified, the nature of cross-reactive humoral responses induced by natural infection with ancestral SARS-CoV-2 strains remains incompletely understood. Here, we isolated 105 S-specific monoclonal antibodies (mAbs) from individuals recovered from prototype SARS-CoV-2 infection. Of these, 30 mAbs cross-recognized SARS-CoV-1, including 25 RBD-directed mAbs, of which 12 displayed cross-neutralizing activity against both viruses. Among them, mAb 12C2 potently neutralized SARS-CoV-1 and multiple SARS-CoV-2 variants, likely through mechanisms that include inhibition of membrane fusion and potential destabilization of the S trimer. Cryo-electron microscopy revealed that 12C2 engages the outer face of the RBD, overlapping with the epitope recognized by the broadly neutralizing antibody S309 derived from SARS-CoV-1 convalescent. Collectively, these findings demonstrate that ancestral SARS-CoV-2 infection can elicit robust cross-neutralizing antibody responses and provide valuable insights for the design of broadly protective antibodies and vaccines.
External linksViruses / PubMed:41157557 / PubMed Central
MethodsEM (single particle)
Resolution3.02 Å
Structure data

EMDB-67630: Cryo-EM map of SARS-CoV-2 spike complexed with Fab 12C2
Method: EM (single particle) / Resolution: 3.02 Å

Source
  • Severe acute respiratory syndrome coronavirus 2

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