9LF8
Structure of MPXV M1R and mMM1-16 Fab complex
Summary for 9LF8
| Entry DOI | 10.2210/pdb9lf8/pdb |
| Descriptor | mMM1-16 Fab light chain, Entry-fusion complex associated protein OPG095, mMM1-16 Fab heavy chain (3 entities in total) |
| Functional Keywords | mpxv, neutralizing antibody, poxvirus, m1r, viral protein/immune system, viral protein-immune system complex |
| Biological source | Mus musculus More |
| Total number of polymer chains | 12 |
| Total formula weight | 267122.27 |
| Authors | Zhang, Y.,Zhao, R.C.,Wu, L.L.,Wang, Q.H. (deposition date: 2025-01-08, release date: 2025-10-01, Last modification date: 2025-10-22) |
| Primary citation | Zhao, R.,Wu, L.,Zhang, Y.,Ma, J.,Liu, D.,Zheng, Y.,Kong, T.,Ma, R.,Gao, Z.,Chai, Y.,Liu, Y.,Tian, Y.,Xia, Y.,Hou, Y.,Lu, J.,Cong, Z.,Huang, B.,Tan, W.,Xue, J.,Gao, G.F.,Wang, Q. Anti-M1R/B6R antibody characterization and bispecific design for enhanced orthopoxvirus protection. Embo Mol Med, 17:2713-2734, 2025 Cited by PubMed Abstract: The global outbreak of the mpox in humans, caused by the mpox virus (MPXV), underscores the urgent need for safe and effective therapeutics. In this study, we characterized the dominant MPXV immunogens, M1R and B6R, by sequencing monoclonal antibodies (MAbs) from the immunized mice and analyzing their epitopes and functions through in vitro and in vivo assessments of binding and antiviral activities. Several broadly effective anti-M1R and anti-B6R neutralizing MAbs were identified and they exhibited enhanced antiviral effects against MPXV or vaccinia virus (VACV) when used in antibody cocktail and bispecific antibody designs. Notably, the VH-CH1 switch region-inserting format of bispecific antibodies exhibited robust protective efficacy against VACV in a mouse model. Collectively, our study characterized the epitope and functional maps of anti-M1R and anti-B6R MAbs and developed promising broad-spectrum antibody candidates for the treatment of MPXV and other orthopoxvirus infections. PubMed: 40921877DOI: 10.1038/s44321-025-00299-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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