9OGM
BG505 MD39.3 Env gp151 MPER nanodisc in complex with 10E8, BG18 and VRC01 Fabs (1x 10E8 Fab)
This is a non-PDB format compatible entry.
Summary for 9OGM
| Entry DOI | 10.2210/pdb9ogm/pdb |
| EMDB information | 70471 |
| Descriptor | BG18 Fab heavy chain, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (18 entities in total) |
| Functional Keywords | mper, hiv-1, broadly neutralizing antibody, viral protein, viral protein-immune system complex, viral protein/immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 17 |
| Total formula weight | 601524.02 |
| Authors | Rantalainen, K.,Ozorowski, G.,Gharpure, A.,Ward, A.B. (deposition date: 2025-05-01, release date: 2025-07-30, Last modification date: 2026-08-26) |
| Primary citation | Rantalainen, K.,Liguori, A.,Ozorowski, G.,Flynn, C.,Steichen, J.M.,Swanson, O.M.,Madden, P.J.,Baboo, S.,Phulera, S.,Gharpure, A.,Lu, D.,Kalyuzhniy, O.,Skog, P.,Terada, S.,Shil, M.,Diedrich, J.K.,Georgeson, E.,Tingle, R.,Eskandarzadeh, S.,Lee, W.H.,Alavi, N.,Goodwin, D.,Kubitz, M.,Amirzehni, S.,Himansu, S.,Sok, D.,Lee, J.H.,Yates 3rd, J.R.,Paulson, J.C.,Crotty, S.,Schiffner, T.,Ward, A.B.,Schief, W.R. Virus glycoprotein nanodisc platform for vaccine analytics. Nat Commun, 17:-, 2026 Cited by PubMed Abstract: Transmembrane glycoproteins of enveloped viruses are targets of neutralizing antibodies and essential vaccine antigens. mRNA-LNP technology allows in vivo expression of transmembrane glycoproteins, but in vitro biophysical characterization of transmembrane antigens and analysis of post-immunization antibody responses typically rely on soluble proteins. Here, we present a platform for assembling transmembrane glycoprotein vaccine candidates into lipid nanodiscs. We demonstrate the utility of nanodiscs in HIV membrane proximal external region (MPER)-targeting vaccine development by binding assays using surface plasmon resonance (SPR), ex vivo B cell sorting with fluorescence-activated cell sorting (FACS), and by determining the structure of a prototypical HIV MPER-targeting immunogen nanodisc in complex with three broadly neutralizing antibodies (bnAbs), including MPER bnAb 10E8, to 3.5 Å by cryogenic electron microscopy (cryo-EM), providing a template for structure-based immunogen design. To demonstrate general applicability we characterize Ebola virus glycoprotein nanodiscs. Overall, the platform offers a tool for accelerating development of next-generation vaccines. PubMed: 41667448DOI: 10.1038/s41467-026-68985-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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