6VO0
BG505 SOSIP.v5.2 in complex with rabbit Fab 43A2
Summary for 6VO0
| Entry DOI | 10.2210/pdb6vo0/pdb |
| EMDB information | 21256 |
| Descriptor | 43A2 light chain, 43A2 heavy chain, Envelope glycoprotein gp120, ... (7 entities in total) |
| Functional Keywords | hiv, env, antibody, viral protein |
| Biological source | Oryctolagus cuniculus (Rabbit) More |
| Total number of polymer chains | 12 |
| Total formula weight | 302023.80 |
| Authors | Nogal, B.,Cottrell, C.A.,Ward, A.B. (deposition date: 2020-01-29, release date: 2020-07-01, Last modification date: 2024-10-16) |
| Primary citation | Nogal, B.,McCoy, L.E.,van Gils, M.J.,Cottrell, C.A.,Voss, J.E.,Andrabi, R.,Pauthner, M.,Liang, C.H.,Messmer, T.,Nedellec, R.,Shin, M.,Turner, H.L.,Ozorowski, G.,Sanders, R.W.,Burton, D.R.,Ward, A.B. HIV envelope trimer-elicited autologous neutralizing antibodies bind a region overlapping the N332 glycan supersite. Sci Adv, 6:eaba0512-eaba0512, 2020 Cited by PubMed Abstract: To date, immunization studies of rabbits with the BG505 SOSIP.664 HIV envelope glycoprotein trimers have revealed the 241/289 glycan hole as the dominant neutralizing antibody epitope. Here, we isolated monoclonal antibodies from a rabbit that did not exhibit glycan hole-dependent autologous serum neutralization. The antibodies did not compete with a previously isolated glycan hole-specific antibody but did compete with N332 glycan supersite broadly neutralizing antibodies. A 3.5-Å cryoEM structure of one of the antibodies in complex with the BG505 SOSIP.v5.2 trimer demonstrated that while the epitope recognized overlapped the N332 glycan supersite by contacting the GDIR motif at the base of V3, primary contacts were located in the variable V1 loop. These data suggest that strain-specific responses to V1 may interfere with broadly neutralizing responses to the N332 glycan supersite and vaccine immunogens may require engineering to minimize these off-target responses or steer them toward a more desirable pathway. PubMed: 32548265DOI: 10.1126/sciadv.aba0512 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.52 Å) |
Structure validation
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