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TitleRational development of a human antibody cocktail that deploys multiple functions to confer Pan-SARS-CoVs protection.
Journal, issue, pagesCell Res, Vol. 31, Issue 1, Page 25-36, Year 2021
Publish dateDec 1, 2020
AuthorsHangping Yao / Yao Sun / Yong-Qiang Deng / Nan Wang / Yongcong Tan / Na-Na Zhang / Xiao-Feng Li / Chao Kong / Yan-Peng Xu / Qi Chen / Tian-Shu Cao / Hui Zhao / Xintian Yan / Lei Cao / Zhe Lv / Dandan Zhu / Rui Feng / Nanping Wu / Wenhai Zhang / Yuhao Hu / Keda Chen / Rong-Rong Zhang / Qingyu Lv / Shihui Sun / Yunhua Zhou / Run Yan / Guan Yang / Xinglu Sun / Chanjuan Liu / Xiangyun Lu / Linfang Cheng / Hongying Qiu / Xing-Yao Huang / Tianhao Weng / Danrong Shi / Weidong Jiang / Junbin Shao / Lei Wang / Jie Zhang / Tao Jiang / Guojun Lang / Cheng-Feng Qin / Lanjuan Li / Xiangxi Wang /
PubMed AbstractStructural principles underlying the composition and synergistic mechanisms of protective monoclonal antibody cocktails are poorly defined. Here, we exploited antibody cooperativity to develop a ...Structural principles underlying the composition and synergistic mechanisms of protective monoclonal antibody cocktails are poorly defined. Here, we exploited antibody cooperativity to develop a therapeutic antibody cocktail against SARS-CoV-2. On the basis of our previously identified humanized cross-neutralizing antibody H014, we systematically analyzed a fully human naive antibody library and rationally identified a potent neutralizing antibody partner, P17, which confers effective protection in animal model. Cryo-EM studies dissected the nature of the P17 epitope, which is SARS-CoV-2 specific and distinctly different from that of H014. High-resolution structure of the SARS-CoV-2 spike in complex with H014 and P17, together with functional investigations revealed that in a two-antibody cocktail, synergistic neutralization was achieved by S1 shielding and conformational locking, thereby blocking receptor attachment and viral membrane fusion, conferring high potency as well as robustness against viral mutation escape. Furthermore, cluster analysis identified a hypothetical 3rd antibody partner for further reinforcing the cocktail as pan-SARS-CoVs therapeutics.
External linksCell Res / PubMed:33262452 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.9 Å
Structure data

EMDB-30482, PDB-7cwl:
SARS-CoV-2 spike protein and P17 fab complex with one RBD in close state
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-30483, PDB-7cwm:
Complex of SARS-CoV-2 spike protein and Fab P17 with one RBD in open state and two RBD in closed state
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-30484, PDB-7cwn:
P17-H014 Fab cocktail in complex with SARS-CoV-2 spike protein
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-30485, PDB-7cwo:
SARS-CoV-2 spike protein RBD and P17 fab complex
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsAnimals / Antibodies, Neutralizing / Antibodies, Viral / COVID-19 / Chlorocebus aethiops / Disease Models, Animal / Epitopes / Humans / SARS-CoV-2 / Single-Chain Antibodies / Vero Cells / VIRAL PROTEIN / Complex / Fab / SARS-CoV-2 spike protein / SARS-CoV-2 spike / Cocktail

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