ArticleMedComm2026
Discovery and Structural Characterization of a Highly Protective Neutralizing Antibody Targeting the Mpox Virus A35R Protein.
Shimeng Bai, Shuo Song, Xin Wang, Yuxin Xiao, Yun Long, Fenfang Wu, Fuxiang Wang, Zhongyi Fan, Jianqing Xu, Maozhou He and 1 more
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In one paragraphArticle in MedComm, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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11 authors.
Shimeng BaiBiotherapy Clinical Research Center Shenzhen Key Laboratory of Pathogen and Immunity National Clinical Research Center for Infectious Disease Shenzhen Third People's Hospital The Second Affiliated Hospital Southern University of Science and Technology Shenzhen P. R. China.ORCID https://orcid.org/0000-0003-4020-1934 Shuo SongBiotherapy Clinical Research Center Shenzhen Key Laboratory of Pathogen and Immunity National Clinical Research Center for Infectious Disease Shenzhen Third People's Hospital The Second Affiliated Hospital Southern University of Science and Technology Shenzhen P. R. China.
Xin WangBiotherapy Clinical Research Center Shenzhen Key Laboratory of Pathogen and Immunity National Clinical Research Center for Infectious Disease Shenzhen Third People's Hospital The Second Affiliated Hospital Southern University of Science and Technology Shenzhen P. R. China.
Yuxin XiaoSchool of Pharmaceutical Science and Technology Hangzhou Institute for Advanced Study University of Chinese Academy of Sciences Hangzhou P. R. China.
Yun LongBiotherapy Clinical Research Center Shenzhen Key Laboratory of Pathogen and Immunity National Clinical Research Center for Infectious Disease Shenzhen Third People's Hospital The Second Affiliated Hospital Southern University of Science and Technology Shenzhen P. R. China.
Fenfang WuBiotherapy Clinical Research Center Shenzhen Key Laboratory of Pathogen and Immunity National Clinical Research Center for Infectious Disease Shenzhen Third People's Hospital The Second Affiliated Hospital Southern University of Science and Technology Shenzhen P. R. China.
Fuxiang WangBiotherapy Clinical Research Center Shenzhen Key Laboratory of Pathogen and Immunity National Clinical Research Center for Infectious Disease Shenzhen Third People's Hospital The Second Affiliated Hospital Southern University of Science and Technology Shenzhen P. R. China.
Zhongyi FanBiotherapy Clinical Research Center Shenzhen Key Laboratory of Pathogen and Immunity National Clinical Research Center for Infectious Disease Shenzhen Third People's Hospital The Second Affiliated Hospital Southern University of Science and Technology Shenzhen P. R. China.ORCID https://orcid.org/0000-0002-1392-534X Jianqing XuClinical Center of Biotherapy Zhongshan Hospital & Institutes of Biomedical Sciences Fudan University Shanghai P. R. China.
Hongzhou LuBiotherapy Clinical Research Center Shenzhen Key Laboratory of Pathogen and Immunity National Clinical Research Center for Infectious Disease Shenzhen Third People's Hospital The Second Affiliated Hospital Southern University of Science and Technology Shenzhen P. R. China.ORCID https://orcid.org/0000-0003-3590-4790 Funding
No grant is acknowledged in the PubMed record.
6 · The paper itselfAbstract
The recent resurgence of the mpox virus (MPXV) has raised global health concerns due to its potential to cause severe illness in vulnerable populations. Targeting the extracellular enveloped virus (EEV) protein A35R is a promising strategy to restrict viral dissemination within the host. In this study, we combined mRNA-LNP immunization with the Beacon Optofluidic system to rapidly screen and isolate high-affinity monoclonal antibodies. One of these antibodies, 17H1, exhibited exceptional neutralization against authentic MPXV. Cryo-electron microscopy (Cryo-EM) analysis revealed that 17H1 binds to a specific epitope at the distal ends of the A35R dimer. The interaction is stabilized by a unique network of hydrogen bonds and salt bridges, particularly involving residue E120, distinguishing its binding mode from previously reported A35R antibodies. Furthermore, 17H1 exhibited complete protective efficacy against MPXV infection in vivo and significantly reduced pulmonary viral load and lung pathogenesis. These findings highlight 17H1 as a promising therapeutic candidate for novel mpox interventions.
Indexed as
A35RCryo‐EM structurempox virus (MPXV)mRNA‐LNPneutralizing antibodytherapeutic protection
Identifiers
PMID42358411
PMCPMC13291558
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