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TitlePotent neutralizing RBD-specific antibody cocktail against SARS-CoV-2 and its mutant.
Journal, issue, pagesMedComm (2020), Vol. 2, Issue 3, Page 442-452, Year 2021
Publish dateJun 24, 2021
AuthorsLina Jia / Yan-Ping Liu / Li-Fei Tian / Chao Xiong / Xin Xu / Honge Qu / Weixi Xiong / Dong Zhou / Feng Wang / Zheng Liu / Xiao-Xue Yan / Wenqing Xu / Lin Tang /
PubMed AbstractThe ongoing pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its variants has posed a serious global public health emergency. Therapeutic interventions or vaccines ...The ongoing pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its variants has posed a serious global public health emergency. Therapeutic interventions or vaccines are urgently needed to treat and prevent the further dissemination of this contagious virus. This study described the identification of neutralizing receptor-binding domain (RBD)-specific antibodies from mice through vaccination with a recombinant SARS-CoV-2 RBD. RBD-targeted monoclonal antibodies (mAbs) with distinct function and epitope recognition were selected to understand SARS-CoV-2 neutralization. High-affinity RBD-specific antibodies exhibited high potency in neutralizing both live and pseudotype SARS-CoV-2 viruses and the SARS-CoV-2 pseudovirus particle containing the spike protein S-RBD mutant (SARS-CoV-2(V367F)). These results demonstrated that these antibodies recognize four distinct groups (I-IV) of epitopes on the RBD and that mAbs targeting group I epitope can be used in combination with mAbs recognizing groups II and/or IV epitope to make mAb cocktails against SARS-CoV-2 and its mutants. Moreover, structural characterization reveals that groups I, III, and IV epitopes are closely located to an RBD hotspot. The identification of RBD-specific antibodies and cocktails may provide an effective therapeutic and prophylactic intervention against SARS-CoV-2 and its isolates.
External linksMedComm (2020) / PubMed:34541573 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 3.8 Å
Structure data

EMDB-30861:
Cryo-electron microscopy density map of the the RBD V367F in complex with MA1ScFv, MA2Fab, and MA5Fab
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-30863:
Cryo-electron microscopy density map of the the RBD in complex with MA1ScFv, MA2Fab
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • Severe acute respiratory syndrome coronavirus 2
  • Homo sapiens (human)
  • Mus musculus (house mouse)

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