9IXV
Cryo-EM structure of MERS-CoV S1-NTD bound with KNIH-88 Fab
Summary for 9IXV
| Entry DOI | 10.2210/pdb9ixv/pdb |
| EMDB information | 60978 |
| Descriptor | Spike glycoprotein, Heavy chain from KNIH-88, monoclonal antibody, Light chain from KNIH-88, monoclonal antibody (3 entities in total) |
| Functional Keywords | monoclonal antibody, mers-cov s1-ntd, knih-88, viral protein-immune system complex, viral protein |
| Biological source | Middle East respiratory syndrome-related coronavirus More |
| Total number of polymer chains | 3 |
| Total formula weight | 85326.64 |
| Authors | |
| Primary citation | Lee, S.Y.,Woo, H.M.,Jeon, H.,Kim, N.,Kim, D.S.,Park, C.K.,Kim, H.J.,Kim, K.C.,Lee, J.Y.,Park, K.,Yoo, Y.,Choi, K.,Lee, H. A Novel Antibody Against the Non-Receptor-Binding Domain Region of Middle East Respiratory Syndrome Coronavirus Spike Protein. J.Infect.Dis., 232:982-992, 2025 Cited by PubMed Abstract: The Middle East respiratory syndrome coronavirus (MERS-CoV) was first identified in 2012 and has since spread worldwide. To date, no vaccines or therapeutics against MERS have been approved for clinical use. The spike (S) protein of MERS-CoV facilitates attachment and fusion with target cell membranes. Therefore, inhibiting S protein attachment represents a key therapeutic strategy for treating early MERS-CoV infection. Herein, we present seven human neutralizing antibodies (KNIH-58, -68, -72, -78, -88, -90, and -95) against MERS-CoV. KNIH-58 and -68 bound to the receptor-binding subdomain (RBD) of the spike protein, while the other five monoclonal antibodies (mAbs) did not. KNIH-88, which targets the non-RBD region, exhibited potent neutralizing activities in vitro and in a transgenic mouse model, with similar results for KNIH-58. Structural analysis of KNIH-88 bound to the spike protein revealed novel epitopes in the non-RBD region. These findings may facilitate therapeutic and prophylactic antibody development against MERS-CoV. PubMed: 40241666DOI: 10.1093/infdis/jiaf202 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.11 Å) |
Structure validation
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