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TitleStructural insight into broadening SARS-CoV-2 neutralization by an antibody cocktail harbouring both NTD and RBD potent antibodies.
Journal, issue, pagesEmerg Microbes Infect, Vol. 13, Issue 1, Page 2406300, Year 2024
Publish dateNov 27, 2024
AuthorsWenling Jiang / Yanan Jiang / Hui Sun / Tingting Deng / Kunyu Yu / Qianjiao Fang / Huimin Ge / Miaoling Lan / Yanling Lin / Zhongyue Fang / Yali Zhang / Lizhi Zhou / Tingting Li / Hai Yu / Qingbing Zheng / Shaowei Li / Ningshao Xia / Ying Gu /
PubMed AbstractThe continual emergence of highly pathogenic novel coronaviruses and their variants has underscored the importance of neutralizing monoclonal antibodies (mAbs) as a pivotal therapeutic approach. In ...The continual emergence of highly pathogenic novel coronaviruses and their variants has underscored the importance of neutralizing monoclonal antibodies (mAbs) as a pivotal therapeutic approach. In the present study, we report the specific neutralizing antibodies 13H7 and 9G11, which target the N-terminal domain (NTD) and receptor-binding domain (RBD) of the SARS-CoV-2, respectively. The comparative analysis observed that 13H7 not only neutralizes early variants of concern (VOCs) but also exhibits neutralizing activity against the Omicron sublineage, including BA.4, BA.5, BQ.1, and BQ.1.1. 9G11, as an RBD antibody, also demonstrated remarkable neutralizing efficacy. A cocktail antibody combining 13H7 and 9G11 with the previously reported 3E2 broaden the neutralization spectrum against new variants of the SARS-CoV-2. We elucidated the cryo-EM structure of the complex, clarifying the mechanism of action of the cocktail antibody combination. Additionally, we also emphasized the molecular mechanism between 13H7 and SARS-CoV-2 NTD, revealing the impact of Y144 and H146 residue deletions and mutations on the neutralizing efficacy of 13H7. Taken together, our findings not only offer novel insights into the combination therapy of NTD and RBD neutralizing mAbs but also lay a theoretical foundation for the development of vaccines targeting NTD antibodies, thus providing valuable understanding of alleviating the emergence of SARS-CoV-2 variants.
External linksEmerg Microbes Infect / PubMed:39470577 / PubMed Central
MethodsEM (single particle)
Resolution2.91 - 3.46 Å
Structure data

EMDB-61825: Structure of SARS-CoV-2 Spike in complex with antibodies 3E2, 9G11 and 13H7 (C1)
Method: EM (single particle) / Resolution: 3.32 Å

62925

9lae

EMDB-62925, PDB-9lae:
Locally refined region of SARS-CoV-2 spike in complex with antibodies 9G11 and 3E2.
Method: EM (single particle) / Resolution: 3.46 Å

EMDB-62926: Structure of SARS-CoV-2 Spike in complex with antibodies 3E2, 9G11 and 13H7.
Method: EM (single particle) / Resolution: 2.91 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • Homo sapiens (human)
  • Mus (mice)
  • mus musculus (house mouse)
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / RBD / Fab / VIRAL PROTEIN-IMMUNE SYSTEM complex

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