9OGL
BG505 MD39.3 SOSIP.664 in complex with 3BC315, BG18 and VRC01 Fabs
This is a non-PDB format compatible entry.
Summary for 9OGL
| Entry DOI | 10.2210/pdb9ogl/pdb |
| EMDB information | 70469 |
| 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)-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, gp41, 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 | 573353.30 |
| Authors | |
| Primary citation | Rantalainen, K.,Liguori, A.,Ozorowski, G.,Flynn, C.,Steichen, J.M.,Swanson, O.,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, J.R.,Paulson, J.C.,Crotty, S.,Schiffner, T.,Ward, A.B.,Schief, W.R. Virus glycoprotein nanodisc platform for vaccine design. Biorxiv, 2025 Cited by PubMed Abstract: Transmembrane glycoproteins of enveloped viruses are the targets of neutralizing antibodies and essential vaccine antigens. mRNA-LNP technology allows in situ production of transmembrane glycoproteins upon immunization, but biophysical characterization of transmembrane antigens and in vitro analysis of post-immunization antibody responses typically rely on soluble proteins. Here, we present a methodological platform for assembling transmembrane glycoprotein vaccine candidates into lipid nanodiscs. We demonstrate the utility of the 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 the MPER bnAb 10E8, to 3.5 Å by cryogenic electron microscopy (cryo-EM), providing a template for structure-based immunogen design for MPER. Overall, the platform offers a tool for accelerating the development of next-generation viral vaccines. PubMed: 40666859DOI: 10.1101/2025.05.02.651272 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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