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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Structure of KSHV glycoprotein B | |||||||||
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Sample |
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Keywords | VIRAL PROTEIN | |||||||||
| Function / homology | Function and homology informationhost cell Golgi membrane / host cell endosome membrane / viral envelope / symbiont entry into host cell / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane Similarity search - Function | |||||||||
| Biological species | ![]() Human gammaherpesvirus 8 / Human herpesvirus 8 strain GK18 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.26 Å | |||||||||
Authors | Fang XY / Sun C / Xie C / Liu Z / Zeng MS | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Adv Sci (Weinh) / Year: 2025Title: Structure and Antigenicity of Kaposi's Sarcoma-Associated Herpesvirus Glycoprotein B. Authors: Xin-Yan Fang / Cong Sun / Chu Xie / Bing-Zhen Cheng / Zheng-Zhou Lu / Ge-Xin Zhao / Sen-Fang Sui / Mu-Sheng Zeng / Zheng Liu / ![]() Abstract: Kaposi's sarcoma-associated herpesvirus (KSHV), a member of the human γ-herpesviruses family, exhibits extensive cellular tropism and is associated with Kaposi's sarcoma and various B-cell ...Kaposi's sarcoma-associated herpesvirus (KSHV), a member of the human γ-herpesviruses family, exhibits extensive cellular tropism and is associated with Kaposi's sarcoma and various B-cell malignancies. Despite its clinical significance, no effective prophylactic vaccines or specific therapeutics are currently available to prevent or treat KSHV infection. Similar to other herpesviruses, KSHV depends on the envelope glycoprotein B (gB) for host receptor recognition and membrane fusion initiation, making gB a prime target for antiviral antibody or vaccine development. In this study, the high-resolution cryo-electron microscopy (cryo-EM) structure of KSHV gB is presented, revealing a unique trimeric conformation resembling the postfusion state observed in other herpesviruses. Additionally, the structure of the non-neutralizing monoclonal antibody 2C4 bound to KSHV gB domain IV is resolved. The comparative sequence and structure analyses reveal significant homology in neutralizing epitopes between KSHV and Epstein-Barr virus (EBV) gB, indicating a potential pathway for the development of broad-spectrum antiviral strategies. These findings provide a foundation for a deeper understanding of KSHV's infectious mechanism and pave the way for the creation of universal interventions against the human γ-herpesviruses. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_38910.map.gz | 61.7 MB | EMDB map data format | |
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| Header (meta data) | emd-38910-v30.xml emd-38910.xml | 20.2 KB 20.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_38910_fsc.xml | 13.2 KB | Display | FSC data file |
| Images | emd_38910.png | 76.9 KB | ||
| Filedesc metadata | emd-38910.cif.gz | 6 KB | ||
| Others | emd_38910_additional_1.map.gz emd_38910_half_map_1.map.gz emd_38910_half_map_2.map.gz | 62.1 MB 115.9 MB 115.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-38910 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-38910 | HTTPS FTP |
-Validation report
| Summary document | emd_38910_validation.pdf.gz | 805.8 KB | Display | EMDB validaton report |
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| Full document | emd_38910_full_validation.pdf.gz | 805.4 KB | Display | |
| Data in XML | emd_38910_validation.xml.gz | 20 KB | Display | |
| Data in CIF | emd_38910_validation.cif.gz | 26.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-38910 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-38910 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8y48MC ![]() 9lldC M: atomic model generated by this map C: citing same article ( |
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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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Map
| File | Download / File: emd_38910.map.gz / Format: CCP4 / Size: 125 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: 0.855 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: local map of protein bottom
| File | emd_38910_additional_1.map | ||||||||||||
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| Annotation | local map of protein bottom | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_38910_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_38910_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : glycoprotein B
| Entire | Name: glycoprotein B |
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| Components |
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-Supramolecule #1: glycoprotein B
| Supramolecule | Name: glycoprotein B / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() Human gammaherpesvirus 8 |
-Macromolecule #1: Envelope glycoprotein B
| Macromolecule | Name: Envelope glycoprotein B / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Human herpesvirus 8 strain GK18 / Strain: GK18 |
| Molecular weight | Theoretical: 73.137594 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MTPRSRLATL GTVILLVCFC AGAAHSRGDT FQTSSSPTPP GSSSKAPTKP GEEASGPKSV DFYQFRVCSA SITGELFRFN LEQTCPDTK DKYHQEGILL VYKKNIVPHI FKVRRYRKIA TSVTVYRGHR ESAITNKYEL PRPVPLYEIS HMDSTYQCFS S MKVNVNGV ...String: MTPRSRLATL GTVILLVCFC AGAAHSRGDT FQTSSSPTPP GSSSKAPTKP GEEASGPKSV DFYQFRVCSA SITGELFRFN LEQTCPDTK DKYHQEGILL VYKKNIVPHI FKVRRYRKIA TSVTVYRGHR ESAITNKYEL PRPVPLYEIS HMDSTYQCFS S MKVNVNGV ENTFTDRDDV NTTVFLQPVE GLTDNIQRYF SQPVIYAEPG RVEATYRVRT TVNCEIVDMI ARSAEPYNYF VT SLGDTVE VSPFCYNESS CSTTPSNKNG LSVQVVLNHT VVTYSDRGTS PTPQNRIFVE TGAYTLSWAS ESKTTAVCPL ALW KTFPRS IQTTHEDSFH FVANEITATF TAPLTPVANF TDTYSCLTSD INTTLNASKA KLASTHVPNG TVQYFHTTGG LYLV WQPMS AINLTHAQGD SGNPTSSPPP SASPMTTSAS RGGSGGASTA AAGGGGSTDN LSYTQLQFAY DKLRDGINQV LEELS RAWC REQVRDNLMW YELSKINPTS VMTAIYGRPV SAKFVGDAIS VTECINVDQS SVNIHKSLRT NSKDVCYARP LVTFKF LNS SNLFTGQLGA RNEIILTNNQ VETCKDTCEH YFITRNETLV YKDYAYLRTI NTTDISTLNT FIALNLSFIQ NIDFKAI EL YSSAEKRLAS SGSHHHHHH UniProtKB: Envelope glycoprotein B |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8.3 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Human gammaherpesvirus 8
Authors
China, 1 items
Citation




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












































Homo sapiens (human)
Processing
FIELD EMISSION GUN

