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TitlePotent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients' B Cells.
Journal, issue, pagesCell, Vol. 182, Issue 1, Page 73-84.e16, Year 2020
Publish dateJul 9, 2020
AuthorsYunlong Cao / Bin Su / Xianghua Guo / Wenjie Sun / Yongqiang Deng / Linlin Bao / Qinyu Zhu / Xu Zhang / Yinghui Zheng / Chenyang Geng / Xiaoran Chai / Runsheng He / Xiaofeng Li / Qi Lv / Hua Zhu / Wei Deng / Yanfeng Xu / Yanjun Wang / Luxin Qiao / Yafang Tan / Liyang Song / Guopeng Wang / Xiaoxia Du / Ning Gao / Jiangning Liu / Junyu Xiao / Xiao-Dong Su / Zongmin Du / Yingmei Feng / Chuan Qin / Chengfeng Qin / Ronghua Jin / X Sunney Xie /
PubMed AbstractThe COVID-19 pandemic urgently needs therapeutic and prophylactic interventions. Here, we report the rapid identification of SARS-CoV-2-neutralizing antibodies by high-throughput single-cell RNA and ...The COVID-19 pandemic urgently needs therapeutic and prophylactic interventions. Here, we report the rapid identification of SARS-CoV-2-neutralizing antibodies by high-throughput single-cell RNA and VDJ sequencing of antigen-enriched B cells from 60 convalescent patients. From 8,558 antigen-binding IgG1 clonotypes, 14 potent neutralizing antibodies were identified, with the most potent one, BD-368-2, exhibiting an IC of 1.2 and 15 ng/mL against pseudotyped and authentic SARS-CoV-2, respectively. BD-368-2 also displayed strong therapeutic and prophylactic efficacy in SARS-CoV-2-infected hACE2-transgenic mice. Additionally, the 3.8 Å cryo-EM structure of a neutralizing antibody in complex with the spike-ectodomain trimer revealed the antibody's epitope overlaps with the ACE2 binding site. Moreover, we demonstrated that SARS-CoV-2-neutralizing antibodies could be directly selected based on similarities of their predicted CDR3 structures to those of SARS-CoV-neutralizing antibodies. Altogether, we showed that human neutralizing antibodies could be efficiently discovered by high-throughput single B cell sequencing in response to pandemic infectious diseases.
External linksCell / PubMed:32425270 / PubMed Central
MethodsEM (single particle)
Resolution3.84 Å
Structure data

30247

7byr

EMDB-30247, PDB-7byr:
BD23-Fab in complex with the S ectodomain trimer
Method: EM (single particle) / Resolution: 3.84 Å

Chemicals

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

Source
  • SARS coronavirus 2
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / SARS-CoV-2 / antigen / RBD / neutralizing antibody

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