9PZ2
Crystal structure of HIV Apex neutralizing Fab Q12QBM-007
Summary for 9PZ2
| Entry DOI | 10.2210/pdb9pz2/pdb |
| Descriptor | Fab Q12QBM-007 heavy chain, Fab Q12QBM-007 light chain (3 entities in total) |
| Functional Keywords | hiv apex neutralizing antibody, immune system |
| Biological source | Macaca mulatta More |
| Total number of polymer chains | 2 |
| Total formula weight | 48153.42 |
| Authors | |
| Primary citation | Guenaga, J.,Adori, M.,Bale, S.,Phulera, S.,Zygouras, I.,Schleich, F.A.,Castro Dopico, X.,Agrawal, S.,Ota, M.,Wilson, R.,Cluff, J.,Dzvelaia, T.,Mandolesi, M.,Lee, W.H.,Walsh, A.A.,Melo, M.B.,Verkoczy, L.,Irvine, D.J.,Corcoran, M.,Wilson, I.A.,Carnathan, D.,Silvestri, G.,Ward, A.B.,Ozorowski, G.,Karlsson Hedestam, G.B.,Wyatt, R.T. Vaccination generates broadly cross-neutralizing antibodies to the HIV Env apex. Nature, 2026 Cited by PubMed Abstract: As a chronically replicating virus, HIV has evolved extreme sequence variability and effective shielding of functionally constrained spike protein determinants by host-derived glycans. Broadly neutralizing antibodies, although rare, can be isolated from people living with HIV, revealing conserved envelope glycoprotein (Env) sites as key targets for vaccine development. One such target is the apex of the Env spike. Here we identify a vaccination strategy using heterologous HIV Env trimers covalently coupled to liposomes for multivalent display that resulted in the elicitation of cross-neutralizing HIV serum antibody responses in all trimer-liposome-immunized non-human primates. Critically, we isolated monoclonal antibodies from multiple macaques that cross-neutralize divergent HIV clinical isolates. High-resolution cryogenic electron microscopy structural analyses of monoclonal antibodies from four different macaques demonstrate that they target the Env trimer apex in a manner highly similar to that of the human-infection-elicited, apex-directed broadly neutralizing antibody PG9, representing a substantial advance in HIV vaccine development. PubMed: 42056526DOI: 10.1038/s41586-026-10429-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.544 Å) |
Structure validation
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