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9YHR

AJ09-110 Fab in complex with HIV-1 Env 5MUT-3fill SOSIP

Summary for 9YHR
Entry DOI10.2210/pdb9yhr/pdb
Related9YHO 9YHQ
EMDB information72969 72970 72971
DescriptorTransmembrane protein gp41, Envelope glycoprotein gp120, AJ09-110 Fab heavy chain, ... (8 entities in total)
Functional Keywordshiv-1, envelope protein, vaccine, immunogen, antibody, bnab, viral protein, viral protein-immune system complex, viral protein/immune system
Biological sourceHuman immunodeficiency virus 1 (HIV-1)
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Total number of polymer chains12
Total formula weight310479.43
Authors
Gavor, E.,Gristick, H.B.,Bjorkman, P.J. (deposition date: 2025-09-30, release date: 2026-05-27)
Primary citationSkelly, 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: 42096521
DOI: 10.1126/science.aec6396
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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PDB entries from 2026-05-27

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