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- EMDB-42363: Cryo-EM structure of the BG505 SOSIPv2 in complex with bNAb 05_B0... -

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Basic information

Entry
Database: EMDB / ID: EMD-42363
TitleCryo-EM structure of the BG505 SOSIPv2 in complex with bNAb 05_B08 Fabs
Map datasharpened map (zflipped)
Sample
  • Complex: Antibody-antigen complex of HIV-1 BG505 SOSIPv2 trimer with 05_B08 Fabs
    • Protein or peptide: Envelope glycoprotein gp160
    • Protein or peptide: BG505 DS-SOSIP glycoprotein gp41
    • Protein or peptide: 05_B08 Fab Heavy Chain
    • Protein or peptide: 05_B08 Light Chain
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
KeywordsHIV-1 / ANTIBODY / CD4-BINDING SITE / IMMUNE COMPLEX / Viral Protein-Immune System complex
Function / homology
Function and homology information


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 ...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 / identical protein binding / membrane
Similarity search - Function
Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120
Similarity search - Domain/homology
Envelope glycoprotein gp160 / Envelope glycoprotein gp160
Similarity search - Component
Biological speciesHomo sapiens (human) / Human immunodeficiency virus 1
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsDeLaitsch AT / Bjorkman PJ
Funding support United States, 1 items
OrganizationGrant numberCountry
Bill & Melinda Gates FoundationINV-002143 United States
CitationJournal: Nat Immunol / Year: 2025
Title: Profiling of HIV-1 elite neutralizer cohort reveals a CD4bs bnAb for HIV-1 prevention and therapy.
Authors: Lutz Gieselmann / Andrew T DeLaitsch / Malena Rohde / Henning Gruell / Christoph Kreer / Meryem Seda Ercanoglu / Harry B Gristick / Philipp Schommers / Elvin Ahmadov / Caelan Radford / ...Authors: Lutz Gieselmann / Andrew T DeLaitsch / Malena Rohde / Henning Gruell / Christoph Kreer / Meryem Seda Ercanoglu / Harry B Gristick / Philipp Schommers / Elvin Ahmadov / Caelan Radford / Andrea Mazzolini / Lily Zhang / Anthony P West / Johanna Worczinski / Anna Momot / Maren L Reichwein / Jacqueline Knüfer / Ricarda Stumpf / Nonhlanhla N Mkhize / Haajira Kaldine / Sinethemba Bhebhe / Sharvari Deshpande / Federico Giovannoni / Erin Stefanutti / Fabio Benigni / Colin Havenar-Daughton / Davide Corti / Arne Kroidl / Anurag Adhikari / Aubin J Nanfack / Georgia E Ambada / Ralf Duerr / Lucas Maganga / Wiston William / Nyanda E Ntinginya / Timo Wolf / Christof Geldmacher / Michael Hoelscher / Clara Lehmann / Penny L Moore / Thierry Mora / Aleksandra M Walczak / Peter B Gilbert / Nicole A Doria-Rose / Yunda Huang / Jesse D Bloom / Michael S Seaman / Pamela J Bjorkman / Florian Klein /
Abstract: Administration of HIV-1 neutralizing antibodies can suppress viremia and prevent infection in vivo. However, clinical use is challenged by envelope diversity and rapid viral escape. Here, we ...Administration of HIV-1 neutralizing antibodies can suppress viremia and prevent infection in vivo. However, clinical use is challenged by envelope diversity and rapid viral escape. Here, we performed single B cell profiling of 32 top HIV-1 elite neutralizers to identify broadly neutralizing antibodies with highest antiviral activity. From 831 expressed monoclonal antibodies, we identified 04_A06, a V1-2-encoded broadly neutralizing antibody to the CD4 binding site with remarkable breadth and potency against multiclade pseudovirus panels (geometric mean half-maximal inhibitory concentration = 0.059 µg ml, breadth = 98.5%, 332 strains). Moreover, 04_A06 was not susceptible to classic CD4 binding site escape variants and maintained full viral suppression in HIV-1-infected humanized mice. Structural analyses revealed an unusually long 11-amino-acid heavy chain insertion that facilitates interprotomer contacts with highly conserved residues on the adjacent gp120 protomer. Finally, 04_A06 demonstrated high activity against contemporaneously circulating viruses from the Antibody-Mediated Prevention trials (geometric mean half-maximal inhibitory concentration = 0.082 µg ml, breadth = 98.4%, 191 virus strains), and in silico modeling for 04_A06LS predicted prevention efficacy of >93%. Thus, 04_A06 will provide unique opportunities for effective treatment and prevention of HIV-1 infection.
History
DepositionOct 16, 2023-
Header (metadata) releaseApr 16, 2025-
Map releaseApr 16, 2025-
UpdateOct 29, 2025-
Current statusOct 29, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_42363.png

Downloads & links

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Map

FileDownload / File: emd_42363.map.gz / Format: CCP4 / Size: 229.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharpened map (zflipped)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 392 pix.
= 326.144 Å		0.83 Å/pix.
x 392 pix.
= 326.144 Å		0.83 Å/pix.
x 392 pix.
= 326.144 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.832 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.18
Minimum - Maximum-0.5053771 - 0.8968245
Average (Standard dev.)0.0009963019 (±0.025240578)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions392392392
Spacing392392392
CellA=B=C: 326.144 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: unsharpened map (zflipped)

Fileemd_42363_additional_1.map
Annotationunsharpened map (zflipped)
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Half map: half map "A" (zflipped)

Fileemd_42363_half_map_1.map
Annotationhalf map "A" (zflipped)
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map "B" (zflipped)

Fileemd_42363_half_map_2.map
Annotationhalf map "B" (zflipped)
Projections & Slices
AxesZYX

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Histogram

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Sample components

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Entire : Antibody-antigen complex of HIV-1 BG505 SOSIPv2 trimer with 05_B0...

EntireName: Antibody-antigen complex of HIV-1 BG505 SOSIPv2 trimer with 05_B08 Fabs
Components
  • Complex: Antibody-antigen complex of HIV-1 BG505 SOSIPv2 trimer with 05_B08 Fabs
    • Protein or peptide: Envelope glycoprotein gp160
    • Protein or peptide: BG505 DS-SOSIP glycoprotein gp41
    • Protein or peptide: 05_B08 Fab Heavy Chain
    • Protein or peptide: 05_B08 Light Chain
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: Antibody-antigen complex of HIV-1 BG505 SOSIPv2 trimer with 05_B0...

SupramoleculeName: Antibody-antigen complex of HIV-1 BG505 SOSIPv2 trimer with 05_B08 Fabs
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Envelope glycoprotein gp160

MacromoleculeName: Envelope glycoprotein gp160 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Human immunodeficiency virus 1
Molecular weightTheoretical: 53.864086 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: NLWVTVYYGV PVWKDAETTL FCASDAKAYE TEKHNVWATH ACVPTDPNPQ EIHLENVTEE FNMWKNNMVE QMHTDIISLW DQSLKPCVK LTPLCVTLQC TNVTNNITDD MRGELKNCSF NMTTELRDKK QKVYSLFYRL DVVQINENQG NRSNNSNKEY R LINCNTSA ...String:
NLWVTVYYGV PVWKDAETTL FCASDAKAYE TEKHNVWATH ACVPTDPNPQ EIHLENVTEE FNMWKNNMVE QMHTDIISLW DQSLKPCVK LTPLCVTLQC TNVTNNITDD MRGELKNCSF NMTTELRDKK QKVYSLFYRL DVVQINENQG NRSNNSNKEY R LINCNTSA ITQACPKVSF EPIPIHYCAP AGFAILKCKD KKFNGTGPCP SVSTVQCTHG IKPVVSTQLL LNGSLAEEEV MI RSENITN NAKNILVQFN TPVQINCTRP NNNTRKSIRI GPGQAFYATG DIIGDIRQAH CNVSKATWNE TLGKVVKQLR KHF GNNTII RFANSSGGDL EVTTHSFNCG GEFFYCNTSG LFNSTWISNT SVQGSNSTGS NDSITLPCRI KQIINMWQRI GQAM YAPPI QGVIRCVSNI TGLILTRDGG STNSTTETFR PGGGDMRDNW RSELYKYKVV KIEPLGVAPT RCKRRVVGRR RRRR

UniProtKB: Envelope glycoprotein gp160

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Macromolecule #2: BG505 DS-SOSIP glycoprotein gp41

MacromoleculeName: BG505 DS-SOSIP glycoprotein gp41 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Human immunodeficiency virus 1
Molecular weightTheoretical: 17.146482 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
AVGIGAVFLG FLGAAGSTMG AASMTLTVQA RNLLSGIVQQ QSNLLRAPEA QQHLLKLTVW GIKQLQARVL AVERYLRDQQ LLGIWGCSG KLICCTNVPW NSSWSNRNLS EIWDNMTWLQ WDKEISNYTQ IIYGLLEESQ NQQEKNEQDL LALD

UniProtKB: Envelope glycoprotein gp160

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Macromolecule #3: 05_B08 Fab Heavy Chain

MacromoleculeName: 05_B08 Fab Heavy Chain / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.648855 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: QVRLMQSGDE VKKPGASVRL SCKADGYEFS DYFLHWVRQA PGQGLEWLGF IRPRLGSVNY SKRFQGRITM TRDMSINTVY MELRSLTSD DTAQYYCARM YDTDSYKFDS WGWGTVVIVS SASTKGPSVF PLAPSSKSTS GGTAALGCLV KDYFPEPVTV S WNSGALTS ...String:
QVRLMQSGDE VKKPGASVRL SCKADGYEFS DYFLHWVRQA PGQGLEWLGF IRPRLGSVNY SKRFQGRITM TRDMSINTVY MELRSLTSD DTAQYYCARM YDTDSYKFDS WGWGTVVIVS SASTKGPSVF PLAPSSKSTS GGTAALGCLV KDYFPEPVTV S WNSGALTS GVHTFPAVLQ SSGLYSLSSV VTVPSSSLGT QTYICNVNHK PSNTKVDKRV EPKSCDKTHH HHHH

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Macromolecule #4: 05_B08 Light Chain

MacromoleculeName: 05_B08 Light Chain / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.264758 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: DSPMTQSPSS LSISVGDRVT ITCRSSQYAA HNVNWYQQRS GKPPKLLIYD TSKLQAGVPS RFRGGGFGTE FTFTISSLQP EDVATYYCQ HYEFFGQGTR LEITRTVAAP SVFIFPPSDE QLKSGTASVV CLLNNFYPRE AKVQWKVDNA LQSGNSQESV T EQDSKDST ...String:
DSPMTQSPSS LSISVGDRVT ITCRSSQYAA HNVNWYQQRS GKPPKLLIYD TSKLQAGVPS RFRGGGFGTE FTFTISSLQP EDVATYYCQ HYEFFGQGTR LEITRTVAAP SVFIFPPSDE QLKSGTASVV CLLNNFYPRE AKVQWKVDNA LQSGNSQESV T EQDSKDST YSLSSTLTLS KADYEKHKVY ACEVTHQGLS SPVTKSFNRG EC

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Macromolecule #11: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 11 / Number of copies: 14 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration4.4 mg/mL
BufferpH: 8
Component:
ConcentrationFormulaName
0.02 MTris-HClTris
0.15 MNaClSodium Chloride
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV / Details: 3s blot, 0 blot force.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 3667 / Average exposure time: 2.0 sec. / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 129686
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

6udj

source_name: PDB, initial_model_type: experimental model

8uki

source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-8ulr:
Cryo-EM structure of the BG505 SOSIPv2 in complex with bNAb 05_B08 Fabs

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