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- EMDB-48346: B25M05 Fab bound to HPV16 L1 pentamer -

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Basic information

Entry
Database: EMDB / ID: EMD-48346
TitleB25M05 Fab bound to HPV16 L1 pentamer
Map dataSharpened map of B25M05 bound to HPV16 L1 pentamer
Sample
  • Complex: HPV16 L1 pentamer bound to B25M05 Fab
    • Protein or peptide: Major capsid protein L1
    • Protein or peptide: B25M05 Fab Heavy Chain
    • Protein or peptide: B25M05 Fab Light Chain
KeywordsHPV / antibody / IMMUNE SYSTEM
Function / homology
Function and homology information


T=7 icosahedral viral capsid / endocytosis involved in viral entry into host cell / virion attachment to host cell / host cell nucleus / structural molecule activity
Similarity search - Function
Major capsid L1 (late) protein, Papillomavirus / Major capsid L1 (late) superfamily, Papillomavirus / L1 (late) protein / Double-stranded DNA virus, group I, capsid
Similarity search - Domain/homology
Major capsid protein L1
Similarity search - Component
Biological speciesHuman papillomavirus 16 / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsHurlburt NK / Singh S / Rodarte JV / Pancera M
Funding support United States, 1 items
OrganizationGrant numberCountry
Other private United States
CitationJournal: PLoS Pathog / Year: 2025
Title: Human monoclonal antibodies to HPV16 show evidence for common developmental pathways and public epitopes.
Authors: Joseph J Carter / Nicholas K Hurlburt / Erin M Scherer / Suruchi Singh / Justas V Rodarte / Robin A Smith / Peter Lewis / Rachel Kinzelman / Jacqueline Kieltyka / Madelyn E Cabãn / Gregory ...Authors: Joseph J Carter / Nicholas K Hurlburt / Erin M Scherer / Suruchi Singh / Justas V Rodarte / Robin A Smith / Peter Lewis / Rachel Kinzelman / Jacqueline Kieltyka / Madelyn E Cabãn / Gregory C Wipf / Marie Pancera / Denise A Galloway /
Abstract: Antibodies to human papillomavirus (HPV) primarily recognize surface exposed residues on five loops of the major capsid protein (L1) that vary significantly among HPV types. We determined which loops ...Antibodies to human papillomavirus (HPV) primarily recognize surface exposed residues on five loops of the major capsid protein (L1) that vary significantly among HPV types. We determined which loops were required for neutralization for 68 HPV16 specific human monoclonal antibodies (mAbs) cloned from participants who received an HPV vaccine and describe molecular features of those antibodies. Chimeric HPV16 pseudovirus (cpsV), each having one surface loop bearing multiple amino acid substitutions, were used to determine neutralization specificity. The HPV16-FG-loop was the loop most frequently required for neutralization (42 of 68, 61.8%), however, all surface loops were required for neutralization by multiple mAbs: HI (13, 19.1%), DE (15, 22.1%), EF (five, 7.4%), BC (four, 5.9%). Antibodies that required multiple loops were common (17, 25.0%). Three mAbs (4.4%) required sequences on the c-terminus of L1 and for another three mAbs the neutralization specificity could not be determined. Two types of mAbs appeared to be overrepresented: ten mAbs used immunoglobin heavy chain variable region 2-70 (IGHV2-70) with immunoglobin light chain variable region 1-40 (IGLV1-40), having characteristic mutations in complementarity determining region two (CDRL2) of the light chain. Cryogenic electron microscopy (Cryo-EM) revealed that two of these antibodies bound five Fabs per capsomer interacting with all five L1-surface loops. The other type of mAbs that appeared to be overrepresented were nine mAbs using IGHV4-34, six of which also used DH3-16*02 with conserved CDRH3 sequences. Cryo-EM for one of these mAbs, that required the FG-loop for neutralization, was shown to bind one Fab per capsomer at the apex, interacting with the DE- and FG-loops, with sequences of the Fab CDRH3 inserted between the DE- and FG-loops from two L1 proteins. These two types of mAbs were found in the four participants suggesting that these antibodies shared developmental pathways and bound to similar immunodominant epitopes on the virus.
History
DepositionDec 18, 2024-
Header (metadata) releaseAug 20, 2025-
Map releaseAug 20, 2025-
UpdateNov 12, 2025-
Current statusNov 12, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_48346.png

Downloads & links

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Map

FileDownload / File: emd_48346.map.gz / Format: CCP4 / Size: 42.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map of B25M05 bound to HPV16 L1 pentamer
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.12 Å/pix.
x 224 pix.
= 251.328 Å		1.12 Å/pix.
x 224 pix.
= 251.328 Å		1.12 Å/pix.
x 224 pix.
= 251.328 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.122 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.7
Minimum - Maximum-3.7184224 - 7.435181
Average (Standard dev.)0.004965778 (±0.28962582)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions224224224
Spacing224224224
CellA=B=C: 251.328 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half map B

Fileemd_48346_half_map_1.map
AnnotationHalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A

Fileemd_48346_half_map_2.map
AnnotationHalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : HPV16 L1 pentamer bound to B25M05 Fab

EntireName: HPV16 L1 pentamer bound to B25M05 Fab
Components
  • Complex: HPV16 L1 pentamer bound to B25M05 Fab
    • Protein or peptide: Major capsid protein L1
    • Protein or peptide: B25M05 Fab Heavy Chain
    • Protein or peptide: B25M05 Fab Light Chain

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Supramolecule #1: HPV16 L1 pentamer bound to B25M05 Fab

SupramoleculeName: HPV16 L1 pentamer bound to B25M05 Fab / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Human papillomavirus 16
Molecular weightTheoretical: 280 KDa

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Macromolecule #1: Major capsid protein L1

MacromoleculeName: Major capsid protein L1 / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Human papillomavirus 16
Molecular weightTheoretical: 47.534574 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: AVVSTDEYVA RTNIYYHAGT SRLLAVGHPY FPIKKPNNNK ILVPKVSGLQ YRVFRIHLPD PNKFGFPDTS FYNPDTQRLV WACVGVEVG RGQPLGVGIS GHPLLNKLDD TENASAYAAN AGVDNRECIS MDYKQTQLCL IGCKPPIGEH WGKGSPCTNV A VQPGDCPP ...String:
AVVSTDEYVA RTNIYYHAGT SRLLAVGHPY FPIKKPNNNK ILVPKVSGLQ YRVFRIHLPD PNKFGFPDTS FYNPDTQRLV WACVGVEVG RGQPLGVGIS GHPLLNKLDD TENASAYAAN AGVDNRECIS MDYKQTQLCL IGCKPPIGEH WGKGSPCTNV A VQPGDCPP LELINTVIQD GDMVDTGFGA MDFTTLQANK SEVPLDICTS ICKYPDYIKM VSEPYGDSLF FYLRREQMFV RH LFNRAGT VGENVPDDLY IKGSGSTANL ASSNYFPTPS GSMVTSDAQI FNKPYWLQRA QGHNNGICWG NQLFVTVVDT TRS TNMSLC AAISTSETTY KNTNFKEYLR HGEEYDLQFI FQLCKITLTA DVMTYIHSMN STILEDWNGG SGGEDPLKKY TFWE VNLKE KFSADLDQFP LGRKFLLQLG L

UniProtKB: Major capsid protein L1

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Macromolecule #2: B25M05 Fab Heavy Chain

MacromoleculeName: B25M05 Fab Heavy Chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.864021 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: QVQLQQWGAG LLKPSETLSL TCAVNGGSFS IYYWSWIRQP PGKGLDWIGE INQSGSTNYN PSLKSRVTMS VDTSKSQFSL RMTSVTAAD TAIYYCARAP RIRWGSYRLK QTNFDSWGQG TLVTVSSRST KGPSVFPLAP SSKSTSGGTA ALGCLVKDYF P EPVTVSWN ...String:
QVQLQQWGAG LLKPSETLSL TCAVNGGSFS IYYWSWIRQP PGKGLDWIGE INQSGSTNYN PSLKSRVTMS VDTSKSQFSL RMTSVTAAD TAIYYCARAP RIRWGSYRLK QTNFDSWGQG TLVTVSSRST KGPSVFPLAP SSKSTSGGTA ALGCLVKDYF P EPVTVSWN SGALTSGVHT FPAVLQSSGL YSLSSVVTVP SSSLGTQTYI CNVNHKPSNT KVDKRVEPKS CDKTHHHHHH

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Macromolecule #3: B25M05 Fab Light Chain

MacromoleculeName: B25M05 Fab Light Chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.902104 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: QSALTQPASV SGSPGQSITI SCTGTSNDVG DYDYVSWYQL HPGKAPKLLI FDVSRRPSGV SDRFSGSKSG DTASLTISGL QAEDEADYY CSSYTGSSTY VFGTGTKVSV LSQPKANPTV TLFPPSSEEL QANKATLVCL ISDFYPGAVT VAWKADSSPV K AGVETTTP ...String:
QSALTQPASV SGSPGQSITI SCTGTSNDVG DYDYVSWYQL HPGKAPKLLI FDVSRRPSGV SDRFSGSKSG DTASLTISGL QAEDEADYY CSSYTGSSTY VFGTGTKVSV LSQPKANPTV TLFPPSSEEL QANKATLVCL ISDFYPGAVT VAWKADSSPV K AGVETTTP SKQSNNKYAA SSYLSLTPEQ WKSHRSYSCQ VTHEGSTVEK TVAPTECS

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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

Concentration0.6 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.8 µm / Nominal magnification: 36000

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

2r5h

Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 83711
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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