+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-31219 | |||||||||
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Title | wild type of O type Foot-and-mouth disease virus | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information L-peptidase / modulation by virus of host chromatin organization / RNA-protein covalent cross-linking / : / ribonucleoside triphosphate phosphatase activity / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / cytoplasmic vesicle membrane / : ...L-peptidase / modulation by virus of host chromatin organization / RNA-protein covalent cross-linking / : / ribonucleoside triphosphate phosphatase activity / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / cytoplasmic vesicle membrane / : / nucleoside-triphosphate phosphatase / regulation of translation / protein complex oligomerization / monoatomic ion channel activity / clathrin-dependent endocytosis of virus by host cell / RNA helicase activity / viral protein processing / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / virion attachment to host cell / structural molecule activity / RNA binding / ATP binding Similarity search - Function | |||||||||
Biological species | Foot-and-mouth disease virus - type O | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Dong H / Lu Y | |||||||||
Funding support | China, 1 items
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Citation | Journal: J Virol / Year: 2021 Title: A Heat-Induced Mutation on VP1 of Foot-and-Mouth Disease Virus Serotype O Enhanced Capsid Stability and Immunogenicity. Authors: Hu Dong / Yuanlu Lu / Yun Zhang / Suyu Mu / Nan Wang / Ping Du / Xiaoying Zhi / Xiaobo Wen / Xiangxi Wang / Shiqi Sun / Yanming Zhang / Huichen Guo / Abstract: Foot-and-mouth disease (FMD) is a highly contagious viral disease affecting cloven-hoofed animals that causes a significant economic burden globally. Vaccination is the most effective FMD control ...Foot-and-mouth disease (FMD) is a highly contagious viral disease affecting cloven-hoofed animals that causes a significant economic burden globally. Vaccination is the most effective FMD control strategy. However, FMD virus (FMDV) particles are prone to dissociate when appropriate physical or chemical conditions are unavailable, such as an incomplete cold chain. Such degraded vaccines result in compromised herd vaccination. Therefore, thermostable FMD particles are needed for use in vaccines. This study generated thermostable FMDV mutants (M3 and M10) by serial passages at high temperature, subsequent amplification, and purification. Both mutants contained an alanine-to-threonine mutation at position 13 in VP1 (A1013T), although M3 contained 3 additional mutations. The selected mutants showed improved stability and immunogenicity in neutralizing antibody titers, compared with the wild-type (wt) virus. The sequencing analysis and cryo-electron microscopy showed that the mutation of alanine to threonine at the 13th amino acid in the VP1 protein (A1013T) is critical for the capsid stability of FMDV. Virus-like particles containing A1013T (VLP) also showed significantly improved stability to heat treatment. This study demonstrated that Thr at the 13th amino acid of VP1 could stabilize the capsid of FMDV. Our findings will facilitate the development of a stable vaccine against FMDV serotype O. Foot-and-mouth disease (FMD) serotype O is one of the global epidemic serotypes and causes significant economic loss. Vaccination plays a key role in the prevention and control of FMD. However, the success of vaccination mainly depends on the quality of the vaccine. Here, the thermostable FMD virus (FMDV) mutants (M3 and M10) were selected through thermal screening at high temperatures with improved stability and immunogenicity compared with the wild-type virus. The results of multisequence alignment and cryo-electron microscopy (cryo-EM) analysis showed that the Thr substitution at the 13th amino acid in the VP1 protein is critical for the capsid stability of FMDV. For thermolabile type O FMDV, this major discovery will aid the development of its thermostable 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_31219.map.gz | 92 MB | EMDB map data format | |
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Header (meta data) | emd-31219-v30.xml emd-31219.xml | 12.1 KB 12.1 KB | Display Display | EMDB header |
Images | emd_31219.png | 190.1 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31219 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31219 | HTTPS FTP |
-Related structure data
Related structure data | 7enpMC 7enoC 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_31219.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 1.34 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 : Foot-and-mouth disease virus - type O
Entire | Name: Foot-and-mouth disease virus - type O |
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Components |
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-Supramolecule #1: Foot-and-mouth disease virus - type O
Supramolecule | Name: Foot-and-mouth disease virus - type O / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 12118 / Sci species name: Foot-and-mouth disease virus - type O / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: VP1 of O type FMDV capsid protein
Macromolecule | Name: VP1 of O type FMDV capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Foot-and-mouth disease virus - type O |
Molecular weight | Theoretical: 23.20558 KDa |
Sequence | String: TTSTGESADP VTATVENYGG ETQVQRRHHT DVSFILDRFV KVTPKDSINV LDLMQTPSHT LVGALLRTAT YYFADLEVAV KHKGDLTWV PNGAPVAALD NTTNPTAYHK APLTRLALPY TAPHRVLATV YNGKCKYAEG SLPNVRGDLQ VLAQKAARPL P TSFNYGAI ...String: TTSTGESADP VTATVENYGG ETQVQRRHHT DVSFILDRFV KVTPKDSINV LDLMQTPSHT LVGALLRTAT YYFADLEVAV KHKGDLTWV PNGAPVAALD NTTNPTAYHK APLTRLALPY TAPHRVLATV YNGKCKYAEG SLPNVRGDLQ VLAQKAARPL P TSFNYGAI KATRVTELLY RMKRAETYCP RPLLAVHPSA ARHKQKIVAP VKQ |
-Macromolecule #2: VP2 of O type FMDV capsid protein
Macromolecule | Name: VP2 of O type FMDV capsid protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Foot-and-mouth disease virus - type O |
Molecular weight | Theoretical: 24.496586 KDa |
Sequence | String: DKKTEETTLL EDRILTTRNG HTTSTTQSSV GITHGYATAE DFVNGPNTSG LETRVVQAER FFKTHLFDWV TSDPFGRYYL LELPTDHKG VYGSLTDSYA YMRNGWDVEV TAVGNQFNGG CLLVAMVPEL CSIEQRELFQ LTLFPHQFIN PRTNMTAHIK V PFVGVNRY ...String: DKKTEETTLL EDRILTTRNG HTTSTTQSSV GITHGYATAE DFVNGPNTSG LETRVVQAER FFKTHLFDWV TSDPFGRYYL LELPTDHKG VYGSLTDSYA YMRNGWDVEV TAVGNQFNGG CLLVAMVPEL CSIEQRELFQ LTLFPHQFIN PRTNMTAHIK V PFVGVNRY DQYKVHKPWT LVVMVVAPLT VNTEGAPQIK VYANIAPTNV HVAGEFPSKE |
-Macromolecule #3: VP3 of O type FMDV capsid protein
Macromolecule | Name: VP3 of O type FMDV capsid protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Foot-and-mouth disease virus - type O |
Molecular weight | Theoretical: 23.882836 KDa |
Sequence | String: GIFPVACSDG YGGLVTTDPK TADPVYGKVF NPPRNMLPGR FTNLLDVAEA CPTFLHFDGD VPYVTTKTDS DRVLAQFDLS LAAKHMSNT FLAGLAQYYT QYSGTVNLHF MFTGPTDAKA RYMIAYAPPG MEPPKTPEAA AHCIHAEWDT GLNSKFTFSI P YLSAADYA ...String: GIFPVACSDG YGGLVTTDPK TADPVYGKVF NPPRNMLPGR FTNLLDVAEA CPTFLHFDGD VPYVTTKTDS DRVLAQFDLS LAAKHMSNT FLAGLAQYYT QYSGTVNLHF MFTGPTDAKA RYMIAYAPPG MEPPKTPEAA AHCIHAEWDT GLNSKFTFSI P YLSAADYA YTASDAAETT NVQGWVCLFQ ITHGKAEGDA LVVLASAGKD FELRLPVDAR QQ |
-Macromolecule #4: VP4 of O type FMDV capsid
Macromolecule | Name: VP4 of O type FMDV capsid / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Foot-and-mouth disease virus - type O |
Molecular weight | Theoretical: 8.777145 KDa |
Sequence | String: GAGQSSPATG SQNQSGNTGS IINNYYMQQY QNSMDTQLGN NAISGGSNEG STDTTSTHTT NTQNNDWFSK LASSAFSGLF GALLA |
-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 TALOS ARCTICA |
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Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DARK FIELD |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 30.0 e/Å2 |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
-Image processing
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
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Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1043 |