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Cross-neutralization of RBD mutant strains of SARS-CoV-2 by convalescent patient derived antibodies.
Lou, Yan; Zhao, Wenxiang; Wei, Haitao; Chu, Min; Chao, Ruihua; Yao, Hangping; Su, Junwei; Li, Yanan; Li, Xiulan; Cao, Yu; Feng, Yanyan; Wang, Ping; Xia, Yongyang; Shang, Yushuan; Li, Fengping; Ge, Pingju; Zhang, Xinglin; Gao, Wenjing; Song, Gaojie; Du, Bing; Liang, Tingbo; Qiu, Yunqing; Liu, Mingyao.
  • Lou Y; State Key Laboratory for diagnosis and treatment of infectious diseases, Key Laboratory for Drug Evaluation and Clinical Research of Zhejiang Province, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
  • Zhao W; Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
  • Wei H; SymRay Biopharma LLC., Shanghai, China.
  • Chu M; SymRay Biopharma LLC., Shanghai, China.
  • Chao R; SymRay Biopharma LLC., Shanghai, China.
  • Yao H; Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
  • Su J; State Key Laboratory for diagnosis and treatment of infectious diseases, Key Laboratory for Drug Evaluation and Clinical Research of Zhejiang Province, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
  • Li Y; State Key Laboratory for diagnosis and treatment of infectious diseases, Key Laboratory for Drug Evaluation and Clinical Research of Zhejiang Province, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
  • Li X; SymRay Biopharma LLC., Shanghai, China.
  • Cao Y; SymRay Biopharma LLC., Shanghai, China.
  • Feng Y; SymRay Biopharma LLC., Shanghai, China.
  • Wang P; SymRay Biopharma LLC., Shanghai, China.
  • Xia Y; SymRay Biopharma LLC., Shanghai, China.
  • Shang Y; SymRay Biopharma LLC., Shanghai, China.
  • Li F; SymRay Biopharma LLC., Shanghai, China.
  • Ge P; SymRay Biopharma LLC., Shanghai, China.
  • Zhang X; Acrobiosystems Inc., Beijing, China.
  • Gao W; Acrobiosystems Inc., Beijing, China.
  • Song G; Acrobiosystems Inc., Beijing, China.
  • Du B; Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
  • Liang T; Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
  • Qiu Y; State Key Laboratory for diagnosis and treatment of infectious diseases, Key Laboratory for Drug Evaluation and Clinical Research of Zhejiang Province, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
  • Liu M; State Key Laboratory for diagnosis and treatment of infectious diseases, Key Laboratory for Drug Evaluation and Clinical Research of Zhejiang Province, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Biotechnol J ; 16(11): e2100207, 2021 Nov.
Article in English | MEDLINE | ID: covidwho-1351201
ABSTRACT

BACKGROUND:

The emergence of COVID-19 pandemic resulted in an urgent need for the development of therapeutic interventions. Of which, neutralizing antibodies play a crucial role in the prevention and resolution of viral infection.

METHODS:

We generated antibody libraries from 18 different COVID-19 recovered patients and screened neutralizing antibodies to SARS-CoV-2 and its mutants. After 3 rounds of panning, 456 positive phage clones were obtained with high affinity to RBD (receptor binding domain). Clones were then reconstituted into whole human IgG for epitope binning assay and all 19 IgG were classified into 6 different epitope groups or Bins.

RESULTS:

Although all antibodies were found to bind RBD, the antibodies in Bin2 had superior inhibitory ability of the interaction between spike protein and angiotensin converting enzyme 2 receptor (ACE2). Most importantly, the antibodies from Bin2 showed stronger binding affinity or ability to mutant RBDs (N501Y, W463R, R408I, N354D, V367F, and N354D/D364Y) derived from different SARS-CoV-2 strains as well, suggesting the great potential of these antibodies in preventing infection of SARS-CoV-2 and its mutations. Furthermore, such neutralizing antibodies strongly restricted the binding of RBD to hACE2 overexpressed 293T cells. Consistently, these antibodies effectively neutralized wildtype and more transmissible mutant pseudovirus entry into hACE2 overexpressed 293T cells. In Vero-E6 cells, one of these antibodies can even block the entry of live SARS-CoV-2 into cells at 12.5 nM.

CONCLUSIONS:

These results indicate that the neutralizing human antibodies from the patient-derived antibody libraries have the potential to fight SARS-CoV-2 and its mutants in this global pandemic.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 / Antibodies, Viral Type of study: Experimental Studies / Randomized controlled trials Limits: Humans Language: English Journal: Biotechnol J Journal subject: Biotechnology Year: 2021 Document Type: Article Affiliation country: Biot.202100207

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 / Antibodies, Viral Type of study: Experimental Studies / Randomized controlled trials Limits: Humans Language: English Journal: Biotechnol J Journal subject: Biotechnology Year: 2021 Document Type: Article Affiliation country: Biot.202100207