Two noncompeting human neutralizing antibodies targeting MPXV B6 show protective effects against orthopoxvirus infections

Runchu Zhao, Lili Wu, Junqing Sun, Dezhi Liu, Pu Han, Yue Gao, Yi Zhang, Yanli Xu, Xiao Qu, Han Wang, Yan Chai, Zhihai Chen, George F. Gao and Qihui Wang ()
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Runchu Zhao: Institute of Microbiology, Chinese Academy of Sciences
Lili Wu: Institute of Microbiology, Chinese Academy of Sciences
Junqing Sun: Institute of Microbiology, Chinese Academy of Sciences
Dezhi Liu: Institute of Microbiology, Chinese Academy of Sciences
Pu Han: Institute of Microbiology, Chinese Academy of Sciences
Yue Gao: Institute of Microbiology, Chinese Academy of Sciences
Yi Zhang: Institute of Microbiology, Chinese Academy of Sciences
Yanli Xu: Capital Medical University
Xiao Qu: Institute of Microbiology, Chinese Academy of Sciences
Han Wang: Peking University
Yan Chai: Institute of Microbiology, Chinese Academy of Sciences
Zhihai Chen: Capital Medical University
George F. Gao: Institute of Microbiology, Chinese Academy of Sciences
Qihui Wang: Institute of Microbiology, Chinese Academy of Sciences

Nature Communications, 2024, vol. 15, issue 1, 1-11

Abstract: Abstract The recent outbreak of mpox epidemic, caused by monkeypox virus (MPXV), poses a new threat to global public health. Here, we initially assessed the preexisting antibody level to the MPXV B6 protein in vaccinia vaccinees born before the end of the immunization program and then identified two monoclonal antibodies (MAbs), hMB621 and hMB668, targeting distinct epitopes on B6, from one vaccinee. Binding assays demonstrate that both MAbs exhibit broad binding abilities to B6 and its orthologs in vaccinia (VACV), variola (VARV) and cowpox viruses (CPXV). Neutralizing assays reveal that the two MAbs showed potent neutralization against VACV. Animal experiments using a BALB/c female mouse model indicate that the two MAbs showed effective protection against VACV via intraperitoneal injection. Additionally, we determined the complex structure of B6 and hMB668, revealing the structural feature of B6 and the epitope of hMB668. Collectively, our study provides two promising antibody candidates for the treatment of orthopoxvirus infections, including mpox.

Date: 2024
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DOI: 10.1038/s41467-024-48312-2

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