9YIH
V634-136 UCA Fab in complex with HIV-1 Env del4-3fill SOSIP
This is a non-PDB format compatible entry.
Summary for 9YIH
| Entry DOI | 10.2210/pdb9yih/pdb |
| Related | 9YHT |
| EMDB information | 72973 72990 |
| Descriptor | Transmembrane protein gp41, Envelope glycoprotein gp160, V634-136 UCA Fab heavy chain, ... (8 entities in total) |
| Functional Keywords | hiv-1, envelope protein, vaccine, immunogen, antibody, bnab, viral protein, viral protein-immune system complex, viral protein/immune system |
| Biological source | Human immunodeficiency virus 1 More |
| Total number of polymer chains | 8 |
| Total formula weight | 253619.42 |
| Authors | |
| Primary citation | Skelly, A.N.,Gristick, H.B.,Li, H.,Gavor, E.,Connell, A.J.,Kreider, E.F.,Marchitto, L.,Hogarty, M.P.,Newby, M.L.,Allen, J.D.,Liu, W.,West Jr., A.P.,Ayyanathan, K.,Campion, M.S.,Winters, K.,Gordon, C.G.,Osbaldeston, R.A.,Akeley, M.J.,Lewis, E.,Li, Y.,Singh, A.,Cruickshank, K.,Park, Y.,Zhao, C.,Li, X.,Amereh, K.,Van Itallie, E.,Carey, J.W.,Albertus, A.,DeLaitsch, A.T.,Keeffe, J.R.,Lituchy, M.G.,Walsh, A.A.,Morris, D.J.,Habib, R.,Bibollet-Ruche, F.,Mishra, N.,Avillion, G.,Koranda, N.S.,Plante, S.J.,Martella, C.L.,Lora, J.,Wang, E.J.D.,Lewis, M.G.,Martin, M.A.,Nussenzweig, M.C.,Seaman, M.S.,Irvine, D.J.,Wiehe, K.J.,Haynes, B.F.,Wagh, K.,Korber, B.,Andrabi, R.,Crispin, M.,Weissman, D.,Bjorkman, P.J.,Hahn, B.H.,Shaw, G.M. Induction of broadly neutralizing HIV antibodies by a two-step mechanism informs vaccine design. Science, :eaec6396-eaec6396, 2026 Cited by PubMed Abstract: A major obstacle confronting HIV-1 vaccine and cure research is the lack of an outbred animal model for rapid and consistent induction of broadly neutralizing antibodies (bNAbs). We designed an epitope-focused simian-human immunodeficiency virus (SHIV.5MUT) that elicited broad and potent V3-glycan-targeted antibodies within a year of infection in 14 of 22 macaques compared with 0 of 14 control animals. SHIV.5MUT elicited bNAbs by a two-step mechanism, inducing an initial wave of V1-directed antibodies that selected for Envs with shortened, hypoglycosylated V1 loops, which in turn primed V3-glycan bNAb precursors. Rhesus bNAbs were immunogenetically and structurally diverse, closely resembling human V3-glycan bNAbs. Env-bNAb coevolution revealed a diverse repertoire of bNAb precursors and the Env variants that matured them, yielding a molecular blueprint for vaccine design. PubMed: 42096521DOI: 10.1126/science.aec6396 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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