8K0D
Cryo-EM structure of conformation 2 of complex of Nipah virus attachment G with 1E5 neutralizing antibody
Summary for 8K0D
| Entry DOI | 10.2210/pdb8k0d/pdb |
| Related | 8K0C |
| EMDB information | 36760 36761 |
| Descriptor | The heavy chain of 1E5, The light chain of 1E5, Glycoprotein G (3 entities in total) |
| Functional Keywords | henipavirus, attachment glycoprotein tetramer complex, neutralizing antibody, dynamic structures, viral protein |
| Biological source | Macaca mulatta More |
| Total number of polymer chains | 6 |
| Total formula weight | 188852.00 |
| Authors | |
| Primary citation | Fan, P.,Sun, M.,Zhang, X.,Zhang, H.,Liu, Y.,Yao, Y.,Li, M.,Fang, T.,Sun, B.,Chen, Z.,Chi, X.,Chen, L.,Peng, C.,Chen, Z.,Zhang, G.,Ren, Y.,Liu, Z.,Li, Y.,Li, J.,Li, E.,Guan, W.,Li, S.,Gong, R.,Zhang, K.,Yu, C.,Chiu, S. A potent Henipavirus cross-neutralizing antibody reveals a dynamic fusion-triggering pattern of the G-tetramer. Nat Commun, 15:4330-4330, 2024 Cited by PubMed Abstract: The Hendra and Nipah viruses (HNVs) are highly pathogenic pathogens without approved interventions for human use. In addition, the interaction pattern between the attachment (G) and fusion (F) glycoproteins required for virus entry remains unclear. Here, we isolate a panel of Macaca-derived G-specific antibodies that cross-neutralize HNVs via multiple mechanisms. The most potent antibody, 1E5, confers adequate protection against the Nipah virus challenge in female hamsters. Crystallography demonstrates that 1E5 has a highly similar binding pattern to the receptor. In cryo-electron microscopy studies, the tendency of 1E5 to bind to the upper or lower heads results in two distinct quaternary structures of G. Furthermore, we identify the extended outer loop β1S2-β1S3 of G and two pockets on the apical region of fusion (F) glycoprotein as the essential sites for G-F interactions. This work highlights promising drug candidates against HNVs and contributes deeper insights into the viruses. PubMed: 38773072DOI: 10.1038/s41467-024-48601-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.94 Å) |
Structure validation
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