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

Ozorowski, G.,Phulera, S.,Ward, A.B. (deposition date: 2025-04-30, 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

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: 41667448
DOI: 10.1038/s41467-026-68985-1

Experimental method

ELECTRON MICROSCOPY (3.1 Å)