7TY0
Nipah Virus attachment (G) glycoprotein ectodomain in complex with nAH1.3 neutralizing antibody Fab fragment (local refinement of the stalk region)
Summary for 7TY0
| Entry DOI | 10.2210/pdb7ty0/pdb |
| EMDB information | 26163 |
| Descriptor | Glycoprotein G, Igh protein, nAH Fab light chain, ... (7 entities in total) |
| Functional Keywords | niv, nivg, attachment protein, neutralizing antibodies, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein |
| Biological source | Nipah henipavirus More |
| Total number of polymer chains | 8 |
| Total formula weight | 395647.71 |
| Authors | Wang, Z.Q.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),Veesler, D. (deposition date: 2022-02-10, release date: 2022-03-09, Last modification date: 2024-10-16) |
| Primary citation | Wang, Z.,Amaya, M.,Addetia, A.,Dang, H.V.,Reggiano, G.,Yan, L.,Hickey, A.C.,DiMaio, F.,Broder, C.C.,Veesler, D. Architecture and antigenicity of the Nipah virus attachment glycoprotein. Science, 375:1373-1378, 2022 Cited by PubMed Abstract: Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness. The entry of HNVs into host cells requires the attachment (G) and fusion (F) glycoproteins, which are the main targets of antibody responses. To understand viral infection and host immunity, we determined a cryo-electron microscopy structure of the NiV G homotetrameric ectodomain in complex with the nAH1.3 broadly neutralizing antibody Fab fragment. We show that a cocktail of two nonoverlapping G-specific antibodies neutralizes NiV and HeV synergistically and limits the emergence of escape mutants. Analysis of polyclonal serum antibody responses elicited by vaccination of macaques with NiV G indicates that the receptor binding head domain is immunodominant. These results pave the way for implementing multipronged therapeutic strategies against these deadly pathogens. PubMed: 35239409DOI: 10.1126/science.abm5561 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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