[English] 日本語
Yorodumi
- EMDB-61599: Cryo-EM structure of BV gB and FAB 16F9 complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-61599
TitleCryo-EM structure of BV gB and FAB 16F9 complex
Map data
Sample
  • Complex: BV gB and FAB 16F9 complex
    • Protein or peptide: 16F9 VH
    • Protein or peptide: 16F9 VL
    • Protein or peptide: Virion glycoprotein B
KeywordsCryo-EM / MBV gB protein / FAB 16F9 / Hepes virus / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


: / Herpesvirus Glycoprotein B / Herpesvirus Glycoprotein B, PH-like domain 1 / Herpesvirus Glycoprotein B, PH-like domain 2 / Herpesvirus Glycoprotein B, PH-like domain 2 superfamily / Herpesvirus Glycoprotein B ectodomain / Herpesvirus Glycoprotein B / Herpesvirus Glycoprotein B PH-like domain
Similarity search - Domain/homology
Virion glycoprotein B
Similarity search - Component
Biological speciesMacacine alphaherpesvirus 1 (monkey B virus) / Mus musculus (house mouse) / Cercopithecine herpesvirus 1 (monkey B virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.18 Å
AuthorsLi Y / Zheng Q / Li S / Wu Y
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat Commun / Year: 2025
Title: A broadly neutralizing antibody confers cross-genus protection against alphaherpesviruses by inhibiting gB-mediated membrane fusion.
Authors: Guosong Wang / Yu Li / Chongxin Wu / Tian Chen / Mengxuan Gui / Yue Zeng / Hui Sun / Kaiyun Chen / Xiangfeng Xi / Yanbo Yang / Yuchen Jiang / Yanan Jiang / Liqin Liu / Chengyu Yang / Jiarui ...Authors: Guosong Wang / Yu Li / Chongxin Wu / Tian Chen / Mengxuan Gui / Yue Zeng / Hui Sun / Kaiyun Chen / Xiangfeng Xi / Yanbo Yang / Yuchen Jiang / Yanan Jiang / Liqin Liu / Chengyu Yang / Jiarui Xin / Caihong Liu / Yiyi Li / Ningning Huo / Yang Huang / Lina Lin / Hai Yu / Chenghao Huang / Quan Yuan / Shaowei Li / Kegong Tian / Qingbing Zheng / Ningshao Xia / Yixin Chen /
Abstract: The global prevalence and disease burden of alphaherpesviruses infections, including human-infecting viruses such as HSV-1, HSV-2, and VZV, as well as animal-infecting viruses like PRV, BHV, CHV, and ...The global prevalence and disease burden of alphaherpesviruses infections, including human-infecting viruses such as HSV-1, HSV-2, and VZV, as well as animal-infecting viruses like PRV, BHV, CHV, and FHV, highlight the unmet need for more effective and universal antiviral strategies. However, there has been no significant progress in developing broad-spectrum interventions against herpesvirus. Here we report the identification of a broadly neutralizing antibody against alphaherpesviruses, 16F9, which targets the glycoprotein B (gB) of alphaherpesviruses and offers cross-protection against multiple viruses such as HSV-1, HSV-2, and PRV in mice. 16F9 demonstrated robust therapeutic efficacy in various female mouse models of herpesvirus diseases including PRV-induced viral encephalitis, HSV-1-induced viral encephalitis, viral keratitis, cutaneous herpes, and neonatal herpesvirus infections. High-resolution cryo-electron microscopy structures revealed that 16F9 binds a conserved site of vulnerability on Domain I of gB. The binding of 16F9 disrupts the interaction between pre-gB and gHgL complex, thereby preventing viral membrane fusion and blocking viral infection. This study provides a foundation for advancing antiviral strategies and underscores the potential of gB-targeted interventions for combating herpesvirus infections.
History
DepositionSep 20, 2024-
Header (metadata) releaseSep 24, 2025-
Map releaseSep 24, 2025-
UpdateJan 14, 2026-
Current statusJan 14, 2026Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_61599.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.65 Å/pix.
x 480 pix.
= 312. Å
0.65 Å/pix.
x 480 pix.
= 312. Å
0.65 Å/pix.
x 480 pix.
= 312. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.65 Å
Density
Contour LevelBy AUTHOR: 0.078
Minimum - Maximum-0.65456617 - 1.1371108
Average (Standard dev.)0.00072104175 (±0.028144311)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 312.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: #1

Fileemd_61599_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #2

Fileemd_61599_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : BV gB and FAB 16F9 complex

EntireName: BV gB and FAB 16F9 complex
Components
  • Complex: BV gB and FAB 16F9 complex
    • Protein or peptide: 16F9 VH
    • Protein or peptide: 16F9 VL
    • Protein or peptide: Virion glycoprotein B

-
Supramolecule #1: BV gB and FAB 16F9 complex

SupramoleculeName: BV gB and FAB 16F9 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Macacine alphaherpesvirus 1 (monkey B virus)

-
Macromolecule #1: 16F9 VH

MacromoleculeName: 16F9 VH / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 52.536238 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGRLTSSFLL LIVPAYVLSE VQLQQSGPEL VKPGASVKIS CKASGYTFAD YTMHWVKQSH GKSLEWIGYI NPYSLFIDSN QKFKNKATL TVDNSSYTAY MELRSLTSED SAVYYCARFP PYYGFDSHFD YWGQGTALTV SSAKTTPPSV YPLAPGCGDT T GSSVTLGC ...String:
MGRLTSSFLL LIVPAYVLSE VQLQQSGPEL VKPGASVKIS CKASGYTFAD YTMHWVKQSH GKSLEWIGYI NPYSLFIDSN QKFKNKATL TVDNSSYTAY MELRSLTSED SAVYYCARFP PYYGFDSHFD YWGQGTALTV SSAKTTPPSV YPLAPGCGDT T GSSVTLGC LVKGYFPESV TVTWNSGSLS SSVHTFPALL QSGLYTMSSS VTVPSSTWPS QTVTCSVAHP ASSTTVDKKL EP SGPISTI NPCPPCKECH KCPAPNLEGG PSVFIFPPNI KDVLMISLTP KVTCVVVDVS EDDPDVRISW FVNNVEVHTA QTQ THREDY NSTIRVVSAL PIQHQDWMSG KEFKCKVNNK DLPSPIERTI SKIKGLVRAP QVYILPPPAE QLSRKDVSLT CLVV GFNPG DISVEWTSNG HTEENYKDTA PVLDSDGSYF IYSKLDIKTS KWEKTDSFSC NVRHEGLKNY YLKKTISRSP GK

-
Macromolecule #2: 16F9 VL

MacromoleculeName: 16F9 VL / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 25.464201 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGWSCIILFL VATATGVHSQ IVLSQSPAIL SASPGEKVTM TCRASSSVSY IYWYQQKPES SPKPWIYATS NLASGVPGRF SGSGSGTSY SLTISRVEAE DAATYYCQQW SYNPYTFGGG TKLEIRRADA APTVSIFPPS SEQLTSGGAS VVCFLNNFYP K DINVKWKI ...String:
MGWSCIILFL VATATGVHSQ IVLSQSPAIL SASPGEKVTM TCRASSSVSY IYWYQQKPES SPKPWIYATS NLASGVPGRF SGSGSGTSY SLTISRVEAE DAATYYCQQW SYNPYTFGGG TKLEIRRADA APTVSIFPPS SEQLTSGGAS VVCFLNNFYP K DINVKWKI DGSERQNGVL NSWTDQDSKD STYSMSSTLT LTKDEYERHN SYTCEATHKT STSPIVKSFN RNEC

-
Macromolecule #3: Virion glycoprotein B

MacromoleculeName: Virion glycoprotein B / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Cercopithecine herpesvirus 1 (monkey B virus)
Molecular weightTheoretical: 98.79368 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRPRAGPLPL PSPLVPLLAL ALLAATRPLG PAAATPVVSP RASPAPPVPA ATPTFPDDDN DGEAGAAPGA PGTNASVEAG HATLRENLR DIKALDGDAT FYVCPPPTGA TVVQFEQPRP CPRAPDGQNY TEGIAVIFKE NIAPYKFKAT MYYKDVTVSQ V WFGHRYSQ ...String:
MRPRAGPLPL PSPLVPLLAL ALLAATRPLG PAAATPVVSP RASPAPPVPA ATPTFPDDDN DGEAGAAPGA PGTNASVEAG HATLRENLR DIKALDGDAT FYVCPPPTGA TVVQFEQPRP CPRAPDGQNY TEGIAVIFKE NIAPYKFKAT MYYKDVTVSQ V WFGHRYSQ FMGIFEDRAP VPFEEVIDKI NARGVCRSTA KYVRNNMEST AFHRDDDESD MKLKPAKAAT RTSRGWHTTD LK YNPSRIE AFHRYGTTVN CIVEEVEARS VYPYDEFVLA TGDFVYMSPF YGYRDGAHAE HTAYAADRFR QVDGYYERDL STG RRASTP ATRNLLTTPK FTVGWDWAPK RPSVCTLTKW QEVDEMLRAE YGPSFRFSSS ALSTTFTTNR TEYALSRVDL GDCV GREAR EAVDRIFLRR YNGTHVKVGQ VQYYLATGGF LIAYQPLLSN ALVELYVREL LREQERRPGD AAATPKPSAD PPDVE RIKT TSSVEFARLQ FTYDHIQRHV NDMLGRIAIA WCELQNHELT LWNEARKLNP NAIASATVGR RVSARMLGDV MAVSTC VPV TPDNVIMQNS MRVPARPGTC YSRPLVSFRY EEGGPLVEGQ LGEDNEIRLE RDALEPCTVG HRRYFTFGAG YVYFEDY AY SHQLGRADVT TVSTFINLNL TMLEDHEFVP LEVYTRQEIK DSGLLDYTEV QRRNQLHALR FADIDTVIKA DAHAALFA G LYSFFEGLGD VGRAVGKVVM GIVGGVVSAV SGVSSFLSNP FGALAVGLLV LAGLAAAFFA FRYVMRLQRN PMKALYPLT TKELKSDGPS PAGDGGDGAS GGGEEDFDEA KLAQAREMIR YMALVSAMER TEHKARKKGT SALLSAKVTN MVMRKRAKPR YSPLGDTDE EEL

UniProtKB: Virion glycoprotein B

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TECNAI F30
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / 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: 1.8 µm / Nominal defocus min: 0.9 µm
Experimental equipment
Model: Tecnai F30 / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.18 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 109849
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more