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4.8
54 reviewsSUMMARYThe A35 protein, expressed on the enveloped virion of monkeypox (mpox) virus (MPXV), is essential for viralinfection and spread within the host, making it an effective antiviral target. In this study, we demonstrated twohuman anti-A35 monoclonal antibodies (mAbs) displayed potential protection against MPXV in CAST/EiJmice and rhesus macaques. Using cryo-electron microscopy, we determined two high-resolution structuresof the A35 dimer in complex with the fragment of antigen binding of mAb 975 or mAb 981, revealing detailedinteractions at the antigen-antibody interfaces. Structural analysis showed that these structurally conservedmAbs bind to a groove region at the interface of A35 dimer. Overall, we provided a proof of concept for a single administration of anti-A35 mAbs mitigating the pathogenic effects of MPXV infection in rhesus macaques.These human-derived mAbs could be served as antibody drug candidates, and their binding models to theA35 dimer will provide valuable insights for future vaccine design.
