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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | AM12-352 Fab in complex with HIV-1 Env 5MUT-3fill SOSIP | |||||||||
Map data | ||||||||||
Sample |
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Keywords | HIV-1 / Envelope protein / Vaccine / Immunogen / Antibody / bNAb / Viral Protein / VIRAL PROTEIN-IMMUNE SYSTEM complex | |||||||||
| Function / homology | Function and homology informationsymbiont-mediated perturbation of host defense response / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell ...symbiont-mediated perturbation of host defense response / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / structural molecule activity / membrane / identical protein binding Similarity search - Function | |||||||||
| Biological species | ![]() Human immunodeficiency virus 1 / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.5 Å | |||||||||
Authors | Gristick HB / Gavor E / Bjorkman PJ | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Science / Year: 2026Title: Induction of broadly neutralizing HIV antibodies by a two-step mechanism informs vaccine design. Authors: Ashwin N Skelly / Harry B Gristick / Hui Li / Edem Gavor / Andrew J Connell / Edward F Kreider / Lorie Marchitto / Michael P Hogarty / Maddy L Newby / Joel D Allen / Weimin Liu / Anthony P ...Authors: Ashwin N Skelly / Harry B Gristick / Hui Li / Edem Gavor / Andrew J Connell / Edward F Kreider / Lorie Marchitto / Michael P Hogarty / Maddy L Newby / Joel D Allen / Weimin Liu / Anthony P West / Kasirajan Ayyanathan / Mary S Campion / Kaitlyn Winters / Colette G Gordon / Rebecca A Osbaldeston / Macy J Akeley / Emily Lewis / Yingying Li / Ajay Singh / Kendra Cruickshank / Younghoon Park / Chengyan Zhao / Xuduo Li / Khaled Amereh / Elizabeth Van Itallie / John W Carey / Amie Albertus / Andrew T DeLaitsch / Jennifer R Keeffe / Melinda G Lituchy / Agnes A Walsh / Daniel J Morris / Rumi Habib / Frederic Bibollet-Ruche / Nitesh Mishra / Gabriel Avillion / Nicholas S Koranda / Samantha J Plante / Christian L Martella / Jinery Lora / Eric J D Wang / Mark G Lewis / Malcolm A Martin / Michel C Nussenzweig / Michael S Seaman / Darrell J Irvine / Kevin J Wiehe / Barton F Haynes / Kshitij Wagh / Bette Korber / Raiees Andrabi / Max Crispin / Drew Weissman / Pamela J Bjorkman / Beatrice H Hahn / George M Shaw / ![]() 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 ...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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_72986.map.gz | 168.1 MB | EMDB map data format | |
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| Header (meta data) | emd-72986-v30.xml emd-72986.xml | 26.1 KB 26.1 KB | Display Display | EMDB header |
| Images | emd_72986.png | 78.8 KB | ||
| Filedesc metadata | emd-72986.cif.gz | 8.1 KB | ||
| Others | emd_72986_half_map_1.map.gz emd_72986_half_map_2.map.gz | 164.8 MB 164.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-72986 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-72986 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9yidMC ![]() 9yhoC ![]() 9yhqC ![]() 9yhrC ![]() 9yhtC ![]() 9yibC ![]() 9yieC ![]() 9yifC ![]() 9yigC ![]() 9yihC ![]() 9yiiC ![]() 9yijC ![]() 9yikC ![]() 9yilC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_72986.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.87 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_72986_half_map_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: #1
| File | emd_72986_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : HIV-1 Envelope protein
| Entire | Name: HIV-1 Envelope protein |
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| Components |
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-Supramolecule #1: HIV-1 Envelope protein
| Supramolecule | Name: HIV-1 Envelope protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 Details: Stabilized, soluble form of heterotrimeric membrane glycoprotein comprising gp120 and gp41 subunits |
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| Source (natural) | Organism: ![]() Human immunodeficiency virus 1 |
| Molecular weight | Theoretical: 330 KDa |
-Macromolecule #1: Transmembrane protein gp41
| Macromolecule | Name: Transmembrane protein gp41 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Human immunodeficiency virus 1 |
| Molecular weight | Theoretical: 17.134324 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: AVGIGAVSLG FLGAAGSTMG AASMTLTVQA RNLLSGIVQQ QSNLLRAPEP QQHLLKDTHW GIKQLQARVL AVEHYLRDQQ LLGIWGCSG KLICCTNVPW NSSWSNRNLS EIWDNMTWLQ WDKEISNYTQ IIYGLLEESQ NQQEKNEQDL LALD UniProtKB: Envelope glycoprotein gp160 |
-Macromolecule #2: Envelope glycoprotein gp120
| Macromolecule | Name: Envelope glycoprotein gp120 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Human immunodeficiency virus 1 |
| Molecular weight | Theoretical: 53.927047 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: NLWVTVYYGV PVWKDAETTL FCASDAKAYE TEKHNVWATH ACVPTDPNPQ EIHLENVTEE FNMWKNNMVE QMHEDIISLW DQSLKPCVK LTPLCVTLQC TNYTPNLTND MRGELKNCSF NMTTELRDKK QKVYSLFYRL DVVQINENQG NRSNNSNKEY R LINCNTSA ...String: NLWVTVYYGV PVWKDAETTL FCASDAKAYE TEKHNVWATH ACVPTDPNPQ EIHLENVTEE FNMWKNNMVE QMHEDIISLW DQSLKPCVK LTPLCVTLQC TNYTPNLTND MRGELKNCSF NMTTELRDKK QKVYSLFYRL DVVQINENQG NRSNNSNKEY R LINCNTSA CTQACPKVSF EPIPIHYCAP AGFAILKCKN KTFNGTGPCP NVSTVQCTHG IKPVVSTQLL LNGSLAEEEV II RSENITN NAKNILVQLN TPVQINCTRP NNNTVKSIRI GPGQAFYYTG DIIGDIRQAH CNVSKATWNE TLGNVSKQLR KHF GNNTII RFAQSSGGDL EVTTHSFNCG GEFFYCNTSG LFNSTWISNT SVQGSNSTGS NDSITLPCRI KQIINMWQRI GQCM YAPPI QGVIRCVSNI TGLILTRDGG STNSTTETFR PGGGDMRDNW RSELYKYKVV KIEPLGVAPT RCKRRVVGRR RRRR UniProtKB: Envelope glycoprotein gp160 |
-Macromolecule #3: AM12-352 Fab heavy chain
| Macromolecule | Name: AM12-352 Fab heavy chain / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 14.45413 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: VQLQQWGEGR VQPSETLSLP CAVYGGSISD YYWSWIRQPP GEGLEWIAHV DPISPTIDYY NPSFKNRITI SKDTSKNQFS LKLRSVTAA DTAVYYCARA GPLRYYGPWN NQRRFDFWGP GVLVTVSS |
-Macromolecule #4: AM12-352 Fab light chain
| Macromolecule | Name: AM12-352 Fab light chain / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 12.338774 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: DVVMTQSPLS LSITPGQPAS ISCRFSQSLV HSDGNTYLSW YQQKPGQPPR LLIYKVSNRD SGVPDRFSGS GAGTDFTLKI SRLEAEDVG VYYCGQATHW PWTFGQGTKV EIK |
-Macromolecule #8: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 8 / Number of copies: 30 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 2 mg/mL | |||||||||
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| Buffer | pH: 8 Component:
Details: 150 mM NaCl, 20 mM Tris-HCl, pH 8.0 | |||||||||
| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 20 | |||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV | |||||||||
| Details | The sample was purified and monodisperse. |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.2 µm / Nominal defocus min: 0.6 µm |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Human immunodeficiency virus 1
Authors
United States, 2 items
Citation






























Z (Sec.)
Y (Row.)
X (Col.)




































Homo sapiens (human)
Processing
FIELD EMISSION GUN
