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Structure paper

TitleStructural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody.
Journal, issue, pagesScience, Vol. 369, Issue 6510, Page 1505-1509, Year 2020
Publish dateSep 18, 2020
AuthorsZhe Lv / Yong-Qiang Deng / Qing Ye / Lei Cao / Chun-Yun Sun / Changfa Fan / Weijin Huang / Shihui Sun / Yao Sun / Ling Zhu / Qi Chen / Nan Wang / Jianhui Nie / Zhen Cui / Dandan Zhu / Neil Shaw / Xiao-Feng Li / Qianqian Li / Liangzhi Xie / Youchun Wang / Zihe Rao / Cheng-Feng Qin / Xiangxi Wang /
PubMed AbstractThe coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in an unprecedented public health crisis. There are no approved ...The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in an unprecedented public health crisis. There are no approved vaccines or therapeutics for treating COVID-19. Here we report a humanized monoclonal antibody, H014, that efficiently neutralizes SARS-CoV-2 and SARS-CoV pseudoviruses as well as authentic SARS-CoV-2 at nanomolar concentrations by engaging the spike (S) receptor binding domain (RBD). H014 administration reduced SARS-CoV-2 titers in infected lungs and prevented pulmonary pathology in a human angiotensin-converting enzyme 2 mouse model. Cryo-electron microscopy characterization of the SARS-CoV-2 S trimer in complex with the H014 Fab fragment unveiled a previously uncharacterized conformational epitope, which was only accessible when the RBD was in an open conformation. Biochemical, cellular, virological, and structural studies demonstrated that H014 prevents attachment of SARS-CoV-2 to its host cell receptors. Epitope analysis of available neutralizing antibodies against SARS-CoV and SARS-CoV-2 uncovered broad cross-protective epitopes. Our results highlight a key role for antibody-based therapeutic interventions in the treatment of COVID-19.
External linksScience / PubMed:32703908 / PubMed Central
MethodsEM (single particle)
Resolution3.49 - 3.9 Å
Structure data

30325

7cab

EMDB-30325, PDB-7cab:
Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody
Method: EM (single particle) / Resolution: 3.52 Å

30326

7cac

EMDB-30326, PDB-7cac:
SARS-CoV-2 S trimer with one RBD in the open state and complexed with one H014 Fab.
Method: EM (single particle) / Resolution: 3.55 Å

30331

7cah

EMDB-30331, PDB-7cah:
The interface of H014 Fab binds to SARS-CoV-2 S
Method: EM (single particle) / Resolution: 3.9 Å

30332

7cai

EMDB-30332, PDB-7cai:
SARS-CoV-2 S trimer with two RBDs in the open state and complexed with two H014 Fab
Method: EM (single particle) / Resolution: 3.49 Å

30333

7cak

EMDB-30333, PDB-7cak:
SARS-CoV-2 S trimer with three RBD in the open state and complexed with three H014 Fab
Method: EM (single particle) / Resolution: 3.58 Å

Chemicals

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

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / SARS-CoV-2 / Spike glycoprotein / Spike / neutralizing antibodies / neutralizing antibody / SARS-CoV-2 spike glycoprotein

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