9JQV
The crystal structure of SFTSV Gn and SD12 antibody complex
Summary for 9JQV
| Entry DOI | 10.2210/pdb9jqv/pdb |
| Descriptor | Envelopment polyprotein, SD12 heavy chain, SD12 light chain, ... (7 entities in total) |
| Functional Keywords | sftsv, gn, sd12, antibody, severe fever with thrombocytopenia syndrome virus, viral protein/immune system, viral protein-immune system complex |
| Biological source | SFTS virus HB29 More |
| Total number of polymer chains | 6 |
| Total formula weight | 167976.54 |
| Authors | Shi, W.F.,Quan, C.S.,Qi, J.X. (deposition date: 2024-09-28, release date: 2025-06-18, Last modification date: 2025-12-31) |
| Primary citation | Quan, C.,Nie, K.,Ma, D.,Su, C.,Li, L.,Zheng, W.,Yin, C.,Wang, Y.,Yang, P.,Peng, D.,Liu, X.,Li, W.,Liu, W.,Shan, C.,Zheng, J.,Liu, D.,Zhang, H.,Carr, M.J.,Gao, G.F.,Qi, J.,Shi, W. Molecular mechanism of potently neutralizing human monoclonal antibodies against severe fever with thrombocytopenia virus infection. J.Virol., 99:e0053325-e0053325, 2025 Cited by PubMed Abstract: Although severe fever with thrombocytopenia syndrome (SFTS) was first described in China in 2009, the case fatality rate remains >40% among patients with multi-organ failure. To date, no antivirals specifically targeting SFTSV have been approved. We obtained several monoclonal antibodies (mAbs) from SFTS survivors by single-cell RNA-seq. Neutralization and animal experiments were applied to assess the effects of these mAbs and , and co-crystal structures with SFTSV-Gn glycoproteins were determined by X-ray crystallography. The mAbs SD4, SD12, and SD22 targeted the SFTSV-Gn with high neutralizing activities, and, remarkably, SD4 and SD22 exhibited values in the range of 32-83 pM for different viral genotypes. Notably, a single administration (20 mg/kg) of SD4 and SD22 showed 100% protection in mice at day 3 post-inoculation (dpi). Importantly, SD4 also provided 60% protection at a lower dose (0.3 mg/kg) when administered at 3 dpi. The crystallographic structures of SD4, SD22, and SD12 with Gn were determined at 3.3 Å, 2.8 Å, and 2.4 Å, respectively, which revealed that they recognized a conserved antigenic epitope around the hexon wellhead edge. These human-derived mAbs have significant therapeutic potential for severe SFTS cases and provide a basis for rational antibody-based vaccine designs and clinical trials. PubMed: 40539781DOI: 10.1128/jvi.00533-25 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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