+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-0880 | |||||||||
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Title | The atomic structure of varicella-zoster virus A-capsid | |||||||||
Map data | Cryo-EM structure of varicella-zoster virus A-capsid | |||||||||
Sample |
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Keywords | Herpesvirus / varicella-zoster virus / capsid / VIRUS | |||||||||
Function / homology | Function and homology information T=16 icosahedral viral capsid / viral capsid assembly / viral process / viral capsid / host cell nucleus / structural molecule activity / DNA binding Similarity search - Function | |||||||||
Biological species | Human herpesvirus 3 (Varicella-zoster virus) / Human alphaherpesvirus 3 (Varicella-zoster virus) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.4 Å | |||||||||
Authors | Zheng Q / Li S | |||||||||
Citation | Journal: Nat Microbiol / Year: 2020 Title: Near-atomic cryo-electron microscopy structures of varicella-zoster virus capsids. Authors: Wei Wang / Qingbing Zheng / Dequan Pan / Hai Yu / Wenkun Fu / Jian Liu / Maozhou He / Rui Zhu / Yuze Cai / Yang Huang / Zhenghui Zha / Zhenqin Chen / Xiangzhong Ye / Jinle Han / Yuqiong Que ...Authors: Wei Wang / Qingbing Zheng / Dequan Pan / Hai Yu / Wenkun Fu / Jian Liu / Maozhou He / Rui Zhu / Yuze Cai / Yang Huang / Zhenghui Zha / Zhenqin Chen / Xiangzhong Ye / Jinle Han / Yuqiong Que / Ting Wu / Jun Zhang / Shaowei Li / Hua Zhu / Z Hong Zhou / Tong Cheng / Ningshao Xia / Abstract: Varicella-zoster virus (VZV) is a medically important human herpesvirus that causes chickenpox and shingles, but its cell-associated nature has hindered structure studies. Here we report the cryo- ...Varicella-zoster virus (VZV) is a medically important human herpesvirus that causes chickenpox and shingles, but its cell-associated nature has hindered structure studies. Here we report the cryo-electron microscopy structures of purified VZV A-capsid and C-capsid, as well as of the DNA-containing capsid inside the virion. Atomic models derived from these structures show that, despite enclosing a genome that is substantially smaller than those of other human herpesviruses, VZV has a similarly sized capsid, consisting of 955 major capsid protein (MCP), 900 small capsid protein (SCP), 640 triplex dimer (Tri2) and 320 triplex monomer (Tri1) subunits. The VZV capsid has high thermal stability, although with relatively fewer intra- and inter-capsid protein interactions and less stably associated tegument proteins compared with other human herpesviruses. Analysis with antibodies targeting the N and C termini of the VZV SCP indicates that the hexon-capping SCP-the largest among human herpesviruses-uses its N-terminal half to bridge hexon MCP subunits and possesses a C-terminal flexible half emanating from the inner rim of the upper hexon channel into the tegument layer. Correlation of these structural features and functional observations provide insights into VZV assembly and pathogenesis and should help efforts to engineer gene delivery and anticancer vectors based on the currently available VZV vaccine. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_0880.map.gz | 7.3 GB | EMDB map data format | |
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Header (meta data) | emd-0880-v30.xml emd-0880.xml | 14.7 KB 14.7 KB | Display Display | EMDB header |
Images | emd_0880.png | 185.6 KB | ||
Filedesc metadata | emd-0880.cif.gz | 6.5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0880 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0880 | HTTPS FTP |
-Validation report
Summary document | emd_0880_validation.pdf.gz | 843.1 KB | Display | EMDB validaton report |
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Full document | emd_0880_full_validation.pdf.gz | 842.7 KB | Display | |
Data in XML | emd_0880_validation.xml.gz | 13.5 KB | Display | |
Data in CIF | emd_0880_validation.cif.gz | 15.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0880 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0880 | HTTPS FTP |
-Related structure data
Related structure data | 6lglMC 0881C 6lgnC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_0880.map.gz / Format: CCP4 / Size: 7.8 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Cryo-EM structure of varicella-zoster virus A-capsid | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.307 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Human alphaherpesvirus 3
Entire | Name: Human alphaherpesvirus 3 (Varicella-zoster virus) |
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Components |
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-Supramolecule #1: Human alphaherpesvirus 3
Supramolecule | Name: Human alphaherpesvirus 3 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10335 / Sci species name: Human alphaherpesvirus 3 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No |
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-Macromolecule #1: Major capsid protein
Macromolecule | Name: Major capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 16 / Enantiomer: LEVO |
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Source (natural) | Organism: Human herpesvirus 3 (Varicella-zoster virus) |
Molecular weight | Theoretical: 155.145359 KDa |
Sequence | String: MTTVSCPANV ITTTESDRIA GLFNIPAGII PTGNVLSTIE VCAHRCIFDF FKQIRSDDNS LYSAQFDILL GTYCNTLNFV RFLELGLSV ACICTKFPEL AYVRDGVIQF EVQQPMIARD GPHPVDQPVH NYMVKRIHKR SLSAAFAIAS EALSLLSNTY V DGTEIDSS ...String: MTTVSCPANV ITTTESDRIA GLFNIPAGII PTGNVLSTIE VCAHRCIFDF FKQIRSDDNS LYSAQFDILL GTYCNTLNFV RFLELGLSV ACICTKFPEL AYVRDGVIQF EVQQPMIARD GPHPVDQPVH NYMVKRIHKR SLSAAFAIAS EALSLLSNTY V DGTEIDSS LRIRAIQQMA RNLRTVLDSF ERGTADQLLG VLLEKAPPLS LLSPINKFQP EGHLNRVARA ALLSDLKRRV CA DMFFMTR HAREPRLISA YLSDMVSCTQ PSVMVSRITH TNTRGRQVDG VLVTTATLKR QLLQGILQID DTAADVPVTY GEM VLQGTN LVTALVMGKA VRGMDDVARH LLDITDPNTL NIPSIPPQSN SDSTTAGLPV NARVPADLVI VGDKLVFLEA LERR VYQAT RVAYPLIGNI DITFIMPMGV FQANSMDRYT RHAGDFSTVS EQDPRQFPPQ GIFFYNKDGI LTQLTLRDAM GTICH SSLL DVEATLVALR QQHLDRQCYF GVYVAEGTED TLDVQMGRFM ETWADMMPHH PHWVNEHLTI LQFIAPSNPR LRFELN PAF DFFVAPGDVD LPGPQRPPEA MPTVNATLRI INGNIPVPLC PISFRDCRGT QLGLGRHTMT PATIKAVKDT FEDRAYP TI FYMLEAVIHG NERNFCALLR LLTQCIRGYW EQSHRVAFVN NFHMLMYITT YLGNGELPEV CINIYRDLLQ HVRALRQT I TDFTIQGEGH NGETSEALNN ILTDDTFIAP ILWDCDALIY RDEAARDRLP AIRVSGRNGY QALHFVDMAG HNFQRRDNV LIHGRPVRGD TGQGIPITPH HDREWGILSK IYYYIVIPAF SRGSCCTMGV RYDRLYPALQ AVIVPEIPAD EEAPTTPEDP RHPLHAHQL VPNSLNVYFH NAHLTVDGDA LLTLQELMGD MAERTTAILV SSAPDAGAAT ATTRNMRIYD GALYHGLIMM A YQAYDETI ATGTFFYPVP VNPLFACPEH LASLRGMTNA RRVLAKMVPP IPPFLGANHH ATIRQPVAYH VTHSKSDFNT LT YSLLGGY FKFTPISLTH QLRTGFHPGI AFTVVRQDRF ATEQLLYAER ASESYFVGQI QVHHHDAIGG VNFTLTQPRA HVD LGVGYT AVCATAALRC PLTDMGNTAQ NLFFSRGGVP MLHDNVTESL RRITASGGRL NPTEPLPIFG GLRPATSAGI ARGQ ASVCE FVAMPVSTDL QYFRTACNPR GRASGMLYMG DRDADIEAIM FDHTQSDVAY TDRATLNPWA SQKHSYGDRL YNGTY NLTG ASPIYSPCFK FFTPAEVNTN CNTLDRLLME AKAVASQSST DTEYQFKRPP GSTEMTQDPC GLFQEAYPPL CSSDAA MLR TAHAGETGAD EVHLAQYLIR DASPLRGCLP LPR UniProtKB: Major capsid protein |
-Macromolecule #2: Small capsomere-interacting protein
Macromolecule | Name: Small capsomere-interacting protein / type: protein_or_peptide / ID: 2 / Number of copies: 15 / Enantiomer: LEVO |
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Source (natural) | Organism: Human herpesvirus 3 (Varicella-zoster virus) |
Molecular weight | Theoretical: 24.440119 KDa |
Sequence | String: MTQPASSRVV FDPSNPTTFS VEAIAAYTPV ALIRLLNASG PLQPGHRVDI ADARSIYTVG AAASAARARA NHNANTIRRT AMFAETDPM TWLRPTVGLK RTFNPRIIRP QPPNPSMSLG ISGPTILPQK TQSADQSALQ QPAALAFSGS SPQHPPPQTT S ASVGQQQH ...String: MTQPASSRVV FDPSNPTTFS VEAIAAYTPV ALIRLLNASG PLQPGHRVDI ADARSIYTVG AAASAARARA NHNANTIRRT AMFAETDPM TWLRPTVGLK RTFNPRIIRP QPPNPSMSLG ISGPTILPQK TQSADQSALQ QPAALAFSGS SPQHPPPQTT S ASVGQQQH VVSGSSGQQP QQGAQSSTVQ PTTGSPPAAQ GVPQSTPPPT QNTPQGGKGQ TLSHTGQSGN ASRSRRV UniProtKB: Small capsomere-interacting protein |
-Macromolecule #3: Triplex capsid protein 1
Macromolecule | Name: Triplex capsid protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: Human herpesvirus 3 (Varicella-zoster virus) |
Molecular weight | Theoretical: 54.02818 KDa |
Sequence | String: MGSQPTNSHF TLNEQTLCGT NISLLGNNRF IQIGNGLHMT YAPGFFGNWS RDLTIGPRFG GLNKQPIHVP PKRTETASIQ VTPRSIVIN RMNNIQINPT SIGNPQVTIR LPLNNFKSTT QLIQQVSLTD FFRPDIEHAG SIVLILRHPS DMIGEANTLT Q AGRDPDVL ...String: MGSQPTNSHF TLNEQTLCGT NISLLGNNRF IQIGNGLHMT YAPGFFGNWS RDLTIGPRFG GLNKQPIHVP PKRTETASIQ VTPRSIVIN RMNNIQINPT SIGNPQVTIR LPLNNFKSTT QLIQQVSLTD FFRPDIEHAG SIVLILRHPS DMIGEANTLT Q AGRDPDVL LEGLRNLFNA CTAPWTVGEG GGLRAYVTSL SFIAACRAEE YTDKQAADAN RTAIVSAYGC SRMETRLIRF SE CLRAMVQ CHVFPHRFIS FFGSLLEYTI QDNLCNITAV AKGPQEAART DKTSTRRVTA NIPACVFWDV DKDLHLSADG LKH VFLVFV YTQRRQREGV RLHLALSQLN EQCFGRGIGF LLGRIRAENA AWGTEGVANT HQPYNTRALP LVQLSNDPTS PRCS IGEIT GVNWNLARQR LYQWTGDFRG LPTQLSCMYA AYTLIGTIPS ESVRYTRRME RFGGYNVPTI WLEGVVWGGT NTWNE CYY UniProtKB: Capsid protein |
-Macromolecule #4: Triplex capsid protein 2
Macromolecule | Name: Triplex capsid protein 2 / type: protein_or_peptide / ID: 4 / Number of copies: 10 / Enantiomer: LEVO |
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Source (natural) | Organism: Human herpesvirus 3 (Varicella-zoster virus) |
Molecular weight | Theoretical: 34.421914 KDa |
Sequence | String: MAMPFEIEVL LPGELSPAET SALQKCEGKI ITFSTLRHRA SLVDIALSSY YINGAPPDTL SLLEAYRMRF AAVITRVIPG KLLAHAIGV GTPTPGLFIQ NTSPVDLCNG DYICLLPPVF GSADSIRLDS VGLEIVFPLT IPQTLMREII AKVVARAVER T AAGAQILP ...String: MAMPFEIEVL LPGELSPAET SALQKCEGKI ITFSTLRHRA SLVDIALSSY YINGAPPDTL SLLEAYRMRF AAVITRVIPG KLLAHAIGV GTPTPGLFIQ NTSPVDLCNG DYICLLPPVF GSADSIRLDS VGLEIVFPLT IPQTLMREII AKVVARAVER T AAGAQILP HEVLRGADVI CYNGRRYELE TNLQHRDGSD AAIRTLVLNL MFSINEGCLL LLALIPTLLV QGAHDGYVNL LI QTANCVR ETGQLINIPP MPRIQDGHRR FPIYETISSW ISTSSRLGDT LGTRAILRVC VFDGPSTVHP GDRTAVIQV UniProtKB: Capsid protein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 56.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: EMDB MAP |
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Final reconstruction | Applied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 22983 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
-Atomic model buiding 1
Refinement | Protocol: AB INITIO MODEL / Target criteria: REAL |
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Output model | PDB-6lgl: |