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TitleDevelopment and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 264, Year 2021
Publish dateJan 11, 2021
AuthorsChao Zhang / Yifan Wang / Yuanfei Zhu / Caixuan Liu / Chenjian Gu / Shiqi Xu / Yalei Wang / Yu Zhou / Yanxing Wang / Wenyu Han / Xiaoyu Hong / Yong Yang / Xueyang Zhang / Tingfeng Wang / Cong Xu / Qin Hong / Shutian Wang / Qiaoyu Zhao / Weihua Qiao / Jinkai Zang / Liangliang Kong / Fangfang Wang / Haikun Wang / Di Qu / Dimitri Lavillette / Hong Tang / Qiang Deng / Youhua Xie / Yao Cong / Zhong Huang /
PubMed AbstractThe ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for ...The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 Å resolution, revealing the conformational space of the antigen-antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections.
External linksNat Commun / PubMed:33431876 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 13.5 Å
Structure data

30635

7dcc

EMDB-30635, PDB-7dcc:
S-3C1-F3b structure, all the three RBDs are in the up conformation and each of them associates with a 3C1 Fab
Method: EM (single particle) / Resolution: 4.3 Å

30641

7dcx

EMDB-30641, PDB-7dcx:
S-3C1-F3a structure, two RBDs are up and one RBD is down, each RBD binds with a 3C1 fab.
Method: EM (single particle) / Resolution: 5.9 Å

30642

7dd2

EMDB-30642, PDB-7dd2:
S-3C1-F2 structure, two RBDs are up and one RBD is down, the two up RBD bind with a 3C1 fab.
Method: EM (single particle) / Resolution: 5.6 Å

30649

7dd8

EMDB-30649, PDB-7dd8:
S-3C1-F1 structure, one RBD is up and two RBDs are down, the up RBD binds with a 3C1 fab
Method: EM (single particle) / Resolution: 7.5 Å

30651

7ddd

EMDB-30651, PDB-7ddd:
SARS-Cov2 S protein at close state
Method: EM (single particle) / Resolution: 3.0 Å

30654

7ddn

EMDB-30654, PDB-7ddn:
SARS-Cov2 S protein at open state
Method: EM (single particle) / Resolution: 6.3 Å

30702

7dk4

EMDB-30702, PDB-7dk4:
S-2H2-F3a structure, two RBDs are up and one RBD is down, each RBD binds with a 2H2 Fab.
Method: EM (single particle) / Resolution: 3.8 Å

30703

7dk5

EMDB-30703, PDB-7dk5:
S-2H2-F1 structure, one RBD is up and two RBDs are down, only up RBD binds with a 2H2 Fab
Method: EM (single particle) / Resolution: 13.5 Å

30704

7dk6

EMDB-30704, PDB-7dk6:
S-2H2-F2 structure, two RBDs are up and one RBD is down, each up RBD binds with a 2H2 Fab.
Method: EM (single particle) / Resolution: 4.3 Å

30705

7dk7

EMDB-30705, PDB-7dk7:
S-2H2-F3b structure, three RBDs are up and each RBD binds with a 2H2 Fab.
Method: EM (single particle) / Resolution: 9.7 Å

Source
  • mus musculus (house mouse)
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / SARS-Cov2 S protein

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