8EJH
Lassa virus glycoprotein complex (Josiah) bound to 12.1F Fab
Summary for 8EJH
| Entry DOI | 10.2210/pdb8ejh/pdb |
| EMDB information | 28182 |
| Descriptor | Glycoprotein G1, alpha-D-mannopyranose, Glycoprotein G2, ... (10 entities in total) |
| Functional Keywords | glycoprotein complex, lassa mammarenavirus, lasv, gpc, immune system, viral fusion protein, lassa virus, lineage iv, josiah, 12.1f, viral protein |
| Biological source | Lassa mammarenavirus More |
| Total number of polymer chains | 12 |
| Total formula weight | 317258.04 |
| Authors | Perrett, H.R.,Ward, A.B. (deposition date: 2022-09-16, release date: 2023-06-07, Last modification date: 2024-10-23) |
| Primary citation | Perrett, H.R.,Brouwer, P.J.M.,Hurtado, J.,Newby, M.L.,Liu, L.,Muller-Krauter, H.,Muller Aguirre, S.,Burger, J.A.,Bouhuijs, J.H.,Gibson, G.,Messmer, T.,Schieffelin, J.S.,Antanasijevic, A.,Boons, G.J.,Strecker, T.,Crispin, M.,Sanders, R.W.,Briney, B.,Ward, A.B. Structural conservation of Lassa virus glycoproteins and recognition by neutralizing antibodies. Cell Rep, 42:112524-112524, 2023 Cited by PubMed Abstract: Lassa fever is an acute hemorrhagic fever caused by the zoonotic Lassa virus (LASV). The LASV glycoprotein complex (GPC) mediates viral entry and is the sole target for neutralizing antibodies. Immunogen design is complicated by the metastable nature of recombinant GPCs and the antigenic differences among phylogenetically distinct LASV lineages. Despite the sequence diversity of the GPC, structures of most lineages are lacking. We present the development and characterization of prefusion-stabilized, trimeric GPCs of LASV lineages II, V, and VII, revealing structural conservation despite sequence diversity. High-resolution structures and biophysical characterization of the GPC in complex with GP1-A-specific antibodies suggest their neutralization mechanisms. Finally, we present the isolation and characterization of a trimer-preferring neutralizing antibody belonging to the GPC-B competition group with an epitope that spans adjacent protomers and includes the fusion peptide. Our work provides molecular detail information on LASV antigenic diversity and will guide efforts to design pan-LASV vaccines. PubMed: 37209096DOI: 10.1016/j.celrep.2023.112524 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.71 Å) |
Structure validation
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