+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-34637 | |||||||||
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Title | cocktail of FMDV (A/TUR/14/98) in complex with M678F and M688F | |||||||||
Map data | ||||||||||
Sample |
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Keywords | FMDV / antibody / VIRUS | |||||||||
Function / homology | Function and homology information icosahedral viral capsid / host cell cytoplasm / symbiont entry into host cell / virion attachment to host cell / structural molecule activity / cytoplasm Similarity search - Function | |||||||||
Biological species | Foot-and-mouth disease virus A / Lama glama (llama) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Li HZ / Dong H / Liu P | |||||||||
Funding support | 1 items
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Citation | Journal: Nat Commun / Year: 2024 Title: Foot-and-mouth disease virus antigenic landscape and reduced immunogenicity elucidated in atomic detail. Authors: Haozhou Li / Pan Liu / Hu Dong / Aldo Dekker / Michiel M Harmsen / Huichen Guo / Xiangxi Wang / Shiqi Sun / Abstract: Unlike most other picornaviruses, foot-and-mouth disease (FMD) intact virions (146S) dissociate easily into small pentameric subunits (12S). This causes a dramatically decreased immunogenicity by a ...Unlike most other picornaviruses, foot-and-mouth disease (FMD) intact virions (146S) dissociate easily into small pentameric subunits (12S). This causes a dramatically decreased immunogenicity by a mechanism that remains elusive. Here, we present the high-resolution structures of 12S (3.2 Å) and its immune complex of a single-domain antibody (VHH) targeting the particle interior (3.2 Å), as well as two 146S-specific VHHs complexed to distinct sites on the 146S capsid surface (3.6 Å and 2.9 Å). The antigenic landscape of 146S is depicted using 13 known FMD virus-antibody complexes. Comparison of the immunogenicity of 146S and 12S in pigs, focusing on the resulting antigenic sites and incorporating structural analysis, reveals that dissociation of 146S leads to structural alteration and destruction of multiple epitopes, resulting in significant differences in antibody profiles/lineages induced by 12S and 146S. Furthermore, 146S generates higher synergistic neutralizing antibody titers compared to 12S, whereas both particles induce similar total FMD virus specific antibody titers. This study can guide the structure-based rational design of novel multivalent and broad-spectrum recombinant vaccines for protection against FMD. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_34637.map.gz | 49.8 MB | EMDB map data format | |
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Header (meta data) | emd-34637-v30.xml emd-34637.xml | 18 KB 18 KB | Display Display | EMDB header |
Images | emd_34637.png | 70.2 KB | ||
Filedesc metadata | emd-34637.cif.gz | 5.8 KB | ||
Others | emd_34637_half_map_1.map.gz emd_34637_half_map_2.map.gz | 75.6 MB 75.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-34637 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-34637 | HTTPS FTP |
-Validation report
Summary document | emd_34637_validation.pdf.gz | 974 KB | Display | EMDB validaton report |
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Full document | emd_34637_full_validation.pdf.gz | 973.5 KB | Display | |
Data in XML | emd_34637_validation.xml.gz | 14.9 KB | Display | |
Data in CIF | emd_34637_validation.cif.gz | 17.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-34637 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-34637 | HTTPS FTP |
-Related structure data
Related structure data | 8hbjMC 8hbgC 8hbiC 8heeC 8hegC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_34637.map.gz / Format: CCP4 / Size: 178 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: 1.36 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_34637_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_34637_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : FMDV capsid protein in complex with M678F nab and M688F nab
Entire | Name: FMDV capsid protein in complex with M678F nab and M688F nab |
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Components |
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-Supramolecule #1: FMDV capsid protein in complex with M678F nab and M688F nab
Supramolecule | Name: FMDV capsid protein in complex with M678F nab and M688F nab type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Foot-and-mouth disease virus A |
-Macromolecule #1: M678F nab
Macromolecule | Name: M678F nab / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Lama glama (llama) |
Molecular weight | Theoretical: 12.753181 KDa |
Recombinant expression | Organism: Yeast centromeric expression vector p416GPD (others) |
Sequence | String: QVQLQESGGG LVQAGGSLRL SCVYSGGAYS MGWYRQAPGK QRELVAAITD DGITNYRDTV KGRFTISRDN AKKAVYLQMN SLKPEDTAV YHCNTVRRVA TLSGSSSGSW GQGTQVTVSS |
-Macromolecule #2: M688F nab
Macromolecule | Name: M688F nab / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Lama glama (llama) |
Molecular weight | Theoretical: 13.861437 KDa |
Recombinant expression | Organism: Yeast centromeric expression vector p416GPD (others) |
Sequence | String: QVQLQESGGG LVQAGDSLRL SCVPSVRTSD NYIMGWFRQP PGKEREFVAA IRRSDGTTKY AASVKGRFAI SRDVAKNAAY LQMNSLKAE DTAVYYCAAK YQSTFYSTMD VQYDYWGQGT QVTVSS |
-Macromolecule #3: VP1 of capsid protein
Macromolecule | Name: VP1 of 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 A |
Molecular weight | Theoretical: 23.111094 KDa |
Sequence | String: TTSAGESADP VTTTVENYGG ETQVQRRHHT DVGFIMDRFV KINNTNPTHV IDLMQTHQHG LVGALLRAAT YYFSDLEIVV RHEGNLTWV PNGAPEAALS NAGNPTAYNK APFTRLALPY TAPHRVLATV YNGTSKYSTT GERTRGDLGA LAARVATQLP A SFNFGAIR ...String: TTSAGESADP VTTTVENYGG ETQVQRRHHT DVGFIMDRFV KINNTNPTHV IDLMQTHQHG LVGALLRAAT YYFSDLEIVV RHEGNLTWV PNGAPEAALS NAGNPTAYNK APFTRLALPY TAPHRVLATV YNGTSKYSTT GERTRGDLGA LAARVATQLP A SFNFGAIR ATDISELLVR MKRAELYCPR PLLAVEVTAQ DRHKQKIIAP AKQ UniProtKB: Genome polyprotein |
-Macromolecule #4: VP2 of capsid protein
Macromolecule | Name: VP2 of capsid protein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Foot-and-mouth disease virus A |
Molecular weight | Theoretical: 24.575779 KDa |
Sequence | String: DKKTEETTLL EDRTLTTRNG HTTSTTQSSV GVTYGYSTGE DHVSGPNTSG LETRVTQAER FFKKHLFNWT TDKPFGHLEK LKLPTDHKG VYGHLVDSFA YMRNGWDVEV SAVGNQFNGG CLLVAMVPEW KKFTPREKYQ LTLFPHQFIS PRTNMTAHIT V PYLGVNRY ...String: DKKTEETTLL EDRTLTTRNG HTTSTTQSSV GVTYGYSTGE DHVSGPNTSG LETRVTQAER FFKKHLFNWT TDKPFGHLEK LKLPTDHKG VYGHLVDSFA YMRNGWDVEV SAVGNQFNGG CLLVAMVPEW KKFTPREKYQ LTLFPHQFIS PRTNMTAHIT V PYLGVNRY DQYKKHKPWT LVVMVVSPLT TSSIGATEIK VYANIAPTHV HVAGELPSKE UniProtKB: Genome polyprotein |
-Macromolecule #5: VP3 of capsid protein
Macromolecule | Name: VP3 of capsid protein / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Foot-and-mouth disease virus A |
Molecular weight | Theoretical: 24.284121 KDa |
Sequence | String: GIVPVACSDG YGGLVTTDPK TADPVYGKVY NPPRTNYPGR FTNLLDVAEA CPTFLCFDDG KPYVVTREDE QRLLAKFDVS LAAKHMSNT YLSGIAQYYA QYSGTINLHF MFTGSTDSKA RYMVAYVPPG VETPPDTPER AAHCIHAEWD TGLNSKFTFS I PYVSAADY ...String: GIVPVACSDG YGGLVTTDPK TADPVYGKVY NPPRTNYPGR FTNLLDVAEA CPTFLCFDDG KPYVVTREDE QRLLAKFDVS LAAKHMSNT YLSGIAQYYA QYSGTINLHF MFTGSTDSKA RYMVAYVPPG VETPPDTPER AAHCIHAEWD TGLNSKFTFS I PYVSAADY AYTASDVAET TNVQGWVCIY QITHGKAQND TLVVSVSAGK DFELRLPIDP RTQ UniProtKB: Genome polyprotein |
-Macromolecule #6: VP4 of capsid protein
Macromolecule | Name: VP4 of capsid protein / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Foot-and-mouth disease virus A |
Molecular weight | Theoretical: 8.778129 KDa |
Sequence | String: GAGQSSPATG SQNQSGNTGS IINNYYMQQY QNSMDTQLGD NAISGGSNEG STDTTSTHTT NTQNNDWFSK LASSAFSGLF GALLA UniProtKB: Genome polyprotein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DIFFRACTION / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 34373 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |