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TitleStructurally Resolved SARS-CoV-2 Antibody Shows High Efficacy in Severely Infected Hamsters and Provides a Potent Cocktail Pairing Strategy.
Journal, issue, pagesCell, Vol. 183, Issue 4, Page 1013-1023.e13, Year 2020
Publish dateNov 12, 2020
AuthorsShuo Du / Yunlong Cao / Qinyu Zhu / Pin Yu / Feifei Qi / Guopeng Wang / Xiaoxia Du / Linlin Bao / Wei Deng / Hua Zhu / Jiangning Liu / Jianhui Nie / Yinghui Zheng / Haoyu Liang / Ruixue Liu / Shuran Gong / Hua Xu / Ayijiang Yisimayi / Qi Lv / Bo Wang / Runsheng He / Yunlin Han / Wenjie Zhao / Yali Bai / Yajin Qu / Xiang Gao / Chenggong Ji / Qisheng Wang / Ning Gao / Weijin Huang / Youchun Wang / X Sunney Xie / Xiao-Dong Su / Junyu Xiao / Chuan Qin /
PubMed AbstractUnderstanding how potent neutralizing antibodies (NAbs) inhibit SARS-CoV-2 is critical for effective therapeutic development. We previously described BD-368-2, a SARS-CoV-2 NAb with high potency; ...Understanding how potent neutralizing antibodies (NAbs) inhibit SARS-CoV-2 is critical for effective therapeutic development. We previously described BD-368-2, a SARS-CoV-2 NAb with high potency; however, its neutralization mechanism is largely unknown. Here, we report the 3.5-Å cryo-EM structure of BD-368-2/trimeric-spike complex, revealing that BD-368-2 fully blocks ACE2 recognition by occupying all three receptor-binding domains (RBDs) simultaneously, regardless of their "up" or "down" conformations. Also, BD-368-2 treats infected adult hamsters at low dosages and at various administering windows, in contrast to placebo hamsters that manifested severe interstitial pneumonia. Moreover, BD-368-2's epitope completely avoids the common binding site of VH3-53/VH3-66 recurrent NAbs, evidenced by tripartite co-crystal structures with RBDs. Pairing BD-368-2 with a potent recurrent NAb neutralizes SARS-CoV-2 pseudovirus at pM level and rescues mutation-induced neutralization escapes. Together, our results rationalized a new RBD epitope that leads to high neutralization potency and demonstrated BD-368-2's therapeutic potential in treating COVID-19.
External linksCell / PubMed:32970990 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.4 - 3.49 Å
Structure data

30374

7chh

EMDB-30374, PDB-7chh:
Cryo-EM structure of the SARS-CoV-2 S-6P in complex with BD-368-2 Fabs
Method: EM (single particle) / Resolution: 3.49 Å

PDB-7ch4:
Crystal structure of the SARS-CoV-2 S RBD in complex with BD-604 Fab
Method: X-RAY DIFFRACTION / Resolution: 3.15 Å

PDB-7ch5:
Crystal structure of the SARS-CoV-2 S RBD in complex with BD-629 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-7chb:
Crystal structure of the SARS-CoV-2 RBD in complex with BD-236 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-7chc:
Crystal structure of the SARS-CoV-2 S RBD in complex with BD-629 Fab and BD-368-2 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.71 Å

PDB-7che:
Crystal structure of the SARS-CoV-2 RBD in complex with BD-236 Fab and BD-368-2 Fab
Method: X-RAY DIFFRACTION / Resolution: 3.416 Å

PDB-7chf:
Crystal structure of the SARS-CoV-2 RBD in complex with BD-604 Fab and BD-368-2 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.674 Å

Chemicals

ChemComp-HOH:
WATER

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

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsPROTEIN BINDING/IMMUNE SYSTEM / Complex / PROTEIN BINDING-IMMUNE SYSTEM complex / ANTIVIRAL PROTEIN/IMMUNE SYSTEM / SARS-Cov-2 / RBD / mAb / ANTIVIRAL PROTEIN / ANTIVIRAL PROTEIN-IMMUNE SYSTEM complex / SARS-CoV-2 Spike / neutralizing antibody

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