Potent SARS-CoV-2 neutralizing antibodies with protective efficacy against newly emerged mutational variants

Tingting Li, Xiaojian Han, Chenjian Gu, Hangtian Guo, Huajun Zhang, Yingming Wang, Chao Hu, Kai Wang, Fengjiang Liu, Feiyang Luo, Yanan Zhang, Jie Hu, Wang Wang, Shenglong Li, Yanan Hao, Meiying Shen, Jingjing Huang, Yingyi Long, Shuyi Song, Ruixin Wu, Song Mu, Qian Chen, Fengxia Gao, Jianwei Wang, Shunhua Long, Luo Li, Yang Wu, Yan Gao, Wei Xu, Xia Cai, Di Qu, Zherui Zhang, Hongqing Zhang, Na Li, Qingzhu Gao, Guiji Zhang, Changlong He, Wei Wang, Xiaoyun Ji, Ni Tang, Zhenghong Yuan, Youhua Xie (), Haitao Yang (), Bo Zhang (), Ailong Huang () and Aishun Jin ()
Additional contact information
Tingting Li: Chongqing Medical University
Xiaojian Han: Chongqing Medical University
Chenjian Gu: Fudan University
Hangtian Guo: ShanghaiTech University
Huajun Zhang: Chinese Academy of Sciences
Yingming Wang: Chongqing Medical University
Chao Hu: Chongqing Medical University
Kai Wang: Chongqing Medical University
Fengjiang Liu: ShanghaiTech University
Feiyang Luo: Chongqing Medical University
Yanan Zhang: Chinese Academy of Sciences
Jie Hu: Chongqing Medical University
Wang Wang: Chongqing Medical University
Shenglong Li: Chongqing Medical University
Yanan Hao: Chongqing Medical University
Meiying Shen: Harbin Medical University Cancer Hospital
Jingjing Huang: Chongqing Medical University
Yingyi Long: Chongqing Medical University
Shuyi Song: Chongqing Medical University
Ruixin Wu: Chongqing Medical University
Song Mu: Chongqing Medical University
Qian Chen: Chongqing Medical University
Fengxia Gao: Chongqing Medical University
Jianwei Wang: Chongqing Medical University
Shunhua Long: Chongqing Medical University
Luo Li: Chongqing Medical University
Yang Wu: Fudan University
Yan Gao: ShanghaiTech University
Wei Xu: Fudan University
Xia Cai: Fudan University
Di Qu: Fudan University
Zherui Zhang: Chinese Academy of Sciences
Hongqing Zhang: Chinese Academy of Sciences
Na Li: Chinese Academy of Sciences
Qingzhu Gao: Chongqing Medical University
Guiji Zhang: Chongqing Medical University
Changlong He: Chongqing Medical University
Wei Wang: Chongqing Medical University
Xiaoyun Ji: Nanjing University
Ni Tang: Chongqing Medical University
Zhenghong Yuan: Fudan University
Youhua Xie: Fudan University
Haitao Yang: ShanghaiTech University
Bo Zhang: Chinese Academy of Sciences
Ailong Huang: Chongqing Medical University
Aishun Jin: Chongqing Medical University

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: Abstract Accumulating mutations in the SARS-CoV-2 Spike (S) protein can increase the possibility of immune escape, challenging the present COVID-19 prophylaxis and clinical interventions. Here, 3 receptor binding domain (RBD) specific monoclonal antibodies (mAbs), 58G6, 510A5 and 13G9, with high neutralizing potency blocking authentic SARS-CoV-2 virus display remarkable efficacy against authentic B.1.351 virus. Surprisingly, structural analysis has revealed that 58G6 and 13G9 both recognize the steric region S470–495 on the RBD, overlapping the E484K mutation presented in B.1.351. Also, 58G6 directly binds to another region S450–458 in the RBD. Significantly, 58G6 and 510A5 both demonstrate prophylactic efficacy against authentic SARS-CoV-2 and B.1.351 viruses in the transgenic mice expressing human ACE2 (hACE2), protecting weight loss and reducing virus loads. Together, we have evidenced 2 potent neutralizing Abs with unique mechanism targeting authentic SARS-CoV-2 mutants, which can be promising candidates to fulfill the urgent needs for the prolonged COVID-19 pandemic.

Date: 2021
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-021-26539-7 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26539-7

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-26539-7

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().