+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-33499 | |||||||||
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Title | Complex of Echo 18 and FcRn at pH7.4 | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Complex / Receptor / VIRUS | |||||||||
Function / homology | Function and homology information IgG immunoglobulin transcytosis in epithelial cells mediated by FcRn immunoglobulin receptor / IgG binding / beta-2-microglobulin binding / endosome membrane / immune response / external side of plasma membrane / extracellular space Similarity search - Function | |||||||||
Biological species | Echovirus E18 / Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.09 Å | |||||||||
Authors | Liu CC / Qu X | |||||||||
Funding support | China, 1 items
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Citation | Journal: mBio / Year: 2022 Title: Human FcRn Is a Two-in-One Attachment-Uncoating Receptor for Echovirus 18. Authors: Xiangpeng Chen / Xiao Qu / Congcong Liu / Yong Zhang / Guigen Zhang / Pu Han / Yali Duan / Qi Li / Liang Wang / Wenjing Ruan / Peiyi Wang / Wensheng Wei / George F Gao / Xin Zhao / Zhengde Xie / Abstract: Virus-receptor interactions determine viral host range and tissue tropism. CD55 and human neonatal Fc receptor (FcRn) were found to be the binding and uncoating receptors for some of the echovirus- ...Virus-receptor interactions determine viral host range and tissue tropism. CD55 and human neonatal Fc receptor (FcRn) were found to be the binding and uncoating receptors for some of the echovirus-related enterovirus species B serotypes in our previous study. Echovirus 18 (E18), as a member of enterovirus species B, is a significant causative agent of aseptic meningitis and viral encephalitis in children. However, it does not use CD55 as a critical host factor. We conducted CRISPR/Cas9 knockout screening to determine the receptors and entry mechanisms and identified FcRn working as a dual-function receptor for E18. Knockout of and , which encode the two subunits of FcRn, prevented infection by E18 and other echoviruses in the same physiological cluster. We then elucidated the underlying molecular mechanism of receptor recognition by E18 using cryogenic electron microscopy. The binding of the FCGRT subunit to the canyon region rotates the residues around the pocket, triggering the release of the pocket factor as observed for other enterovirus species B members. E18 is a member of enterovirus species B. As one of the most common enterovirus serotypes in nonpolio enterovirus detection, it easily infects children and causes various clinical symptoms. Aseptic meningitis and viral encephalitis are the most commonly reported syndromes associated with E18. No effective antiviral drugs or approved vaccines are available. Previous studies showed that CD55 and FcRn were the binding and uncoating receptors for some echoviruses. However, we found that CD55 is not the critical host factor for E18. Thus, we want to determine the receptors and elucidate the entry mechanism of E18. Our findings reveal that FcRn is a two-in-one attachment-uncoating receptor for E18. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_33499.map.gz | 98.5 MB | EMDB map data format | |
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Header (meta data) | emd-33499-v30.xml emd-33499.xml | 25.7 KB 25.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_33499_fsc.xml | 15.3 KB | Display | FSC data file |
Images | emd_33499.png | 150.3 KB | ||
Masks | emd_33499_msk_1.map | 307.5 MB | Mask map | |
Filedesc metadata | emd-33499.cif.gz | 7.1 KB | ||
Others | emd_33499_half_map_1.map.gz emd_33499_half_map_2.map.gz | 227.8 MB 227.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-33499 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-33499 | HTTPS FTP |
-Validation report
Summary document | emd_33499_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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Full document | emd_33499_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | emd_33499_validation.xml.gz | 23 KB | Display | |
Data in CIF | emd_33499_validation.cif.gz | 30.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-33499 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-33499 | HTTPS FTP |
-Related structure data
Related structure data | 7xxaMC 7xxgC 7xxjC 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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-Map
File | Download / File: emd_33499.map.gz / Format: CCP4 / Size: 307.5 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: 1.01 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_33499_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_33499_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_33499_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Echovirus E18
Entire | Name: Echovirus E18 |
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Components |
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-Supramolecule #1: Echovirus E18
Supramolecule | Name: Echovirus E18 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Echovirus E18 |
-Supramolecule #3: FcRn
Supramolecule | Name: FcRn / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 |
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-Supramolecule #2: Homo sapiens
Supramolecule | Name: Homo sapiens / type: virus / ID: 2 / Parent: 1 / Macromolecule list: #1, #3-#5 / NCBI-ID: 9606 / Sci species name: Homo sapiens / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No |
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-Macromolecule #1: VP1
Macromolecule | Name: VP1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Echovirus E18 |
Molecular weight | Theoretical: 35.113328 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: GDNQDRTVAN TQPSGPSNSK EIPALTAVET GHTSQVDPSD TLQTRHVVNF HSRSESTVEN FMGRAACVFM DQYKLNGEET STDNFAVWT INVREMAQLR RKCELFTYMR FDIEMTMVIT SCQDQGTQLE QDMPVLTHQI MYVPPGGPIP AKVDSYEWQT S TNPSVFWT ...String: GDNQDRTVAN TQPSGPSNSK EIPALTAVET GHTSQVDPSD TLQTRHVVNF HSRSESTVEN FMGRAACVFM DQYKLNGEET STDNFAVWT INVREMAQLR RKCELFTYMR FDIEMTMVIT SCQDQGTQLE QDMPVLTHQI MYVPPGGPIP AKVDSYEWQT S TNPSVFWT EGNAPARMSI PFISVGNAYS LFYDGWSHFT QDGTYGYTTL NAMGKLFVRH VNKSSPHQIT STIRVYFKPK HI KAWVPRP PRLCPYINKG DVNFVVTEVT DARKSITDTP HPEHSVLVTR GAFGQQSGAA YIGNYKVVNR HLATH |
-Macromolecule #2: IgG receptor FcRn large subunit p51
Macromolecule | Name: IgG receptor FcRn large subunit p51 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 29.294971 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: LSLLYHLTAV SSPAPGTPAF WVSGWLGPQQ YLSYNSLRGE AEPCGAWVWE NQVSWYWEKE TTDLRIKEKL FLEAFKALGG KGPYTLQGL LGCELGPDNT SVPTAKFALN GEEFMNFDLK QGTWGGDWPE ALAISQRWQQ QDKAANKELT FLLFSCPHRL R EHLERGRG ...String: LSLLYHLTAV SSPAPGTPAF WVSGWLGPQQ YLSYNSLRGE AEPCGAWVWE NQVSWYWEKE TTDLRIKEKL FLEAFKALGG KGPYTLQGL LGCELGPDNT SVPTAKFALN GEEFMNFDLK QGTWGGDWPE ALAISQRWQQ QDKAANKELT FLLFSCPHRL R EHLERGRG NLEWKEPPSM RLKARPSSPG FSVLTCSAFS FYPPELQLRF LRNGLAAGTG QGDFGPNSDG SFHASSSLTV KS GDEHHYC CIVQHAGLAQ PLRVEL UniProtKB: IgG receptor FcRn large subunit p51 |
-Macromolecule #3: VP2
Macromolecule | Name: VP2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Echovirus E18 |
Molecular weight | Theoretical: 28.805348 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: SPSAEECGYS DRVRSMTLGN STITTQESAN VVVGYGEWPS YLSDKEATAE DQPTQPDVAT CRFYTLESVQ WEKSSPGWWW KFPEALKNM GLFGQNMHYH YLGRAGYTIH VQCNASKFHQ GCLLVVCVPE AEMGCADTST TFPATELTTE EEPHVFTSDS I TGKKVQAA ...String: SPSAEECGYS DRVRSMTLGN STITTQESAN VVVGYGEWPS YLSDKEATAE DQPTQPDVAT CRFYTLESVQ WEKSSPGWWW KFPEALKNM GLFGQNMHYH YLGRAGYTIH VQCNASKFHQ GCLLVVCVPE AEMGCADTST TFPATELTTE EEPHVFTSDS I TGKKVQAA VCNAGMGVGV GNLTIFPHQW INLRTNNSAT IVMPYINSVP MDNMFRHYNF TLMIIPFAPL NFNEGATAYV PV TVTIAPM YAEYNGLRLA STQ |
-Macromolecule #4: VP3
Macromolecule | Name: VP3 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Echovirus E18 |
Molecular weight | Theoretical: 26.134842 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: GVPVLNTPGS TQFLTSDDFQ SPSAMPQFDE TPEMHIPGEV RNLMEMAEVD SVVPVNNITG KTKSMEAYQI AVGTGNTDKT KPIFSFQMD PGYSSVLKRT LLGEMLNYYA HWSGSVKLTF LFCGSAMATG KLLISYSPPG ASVPSSRKDA MLGTHIIWDI G LQSSCVLC ...String: GVPVLNTPGS TQFLTSDDFQ SPSAMPQFDE TPEMHIPGEV RNLMEMAEVD SVVPVNNITG KTKSMEAYQI AVGTGNTDKT KPIFSFQMD PGYSSVLKRT LLGEMLNYYA HWSGSVKLTF LFCGSAMATG KLLISYSPPG ASVPSSRKDA MLGTHIIWDI G LQSSCVLC VPWISQSHYR MVQQDPYTSA GYITCWYQTN IVVPPGAPTS CDVLCFASAC NDFSVRLLRD TPFMAQPGKL Q |
-Macromolecule #5: VP4
Macromolecule | Name: VP4 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Echovirus E18 |
Molecular weight | Theoretical: 7.502346 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MGAQVSTQKT GAHETSLNAK GNSIIHYTNI NFYKDAASSA SNRQELQQDP GKFTDPVKDL MVKTLPALN |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 3 mg/mL |
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Buffer | pH: 7.4 |
Grid | Model: EMS Lacey Carbon / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 2 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV Details: blot for 3 seconds and wait for 3 seconds before plunging. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Temperature | Min: 80.0 K / Max: 80.0 K |
Alignment procedure | Coma free - Residual tilt: 100.0 mrad |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Digitization - Frames/image: 1-40 / Number grids imaged: 1 / Number real images: 2028 / Average exposure time: 0.088 sec. / Average electron dose: 1.025 e/Å2 / Details: Images were collected in super-resolution mode. |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 70.0 µm / Calibrated defocus max: 3.5 µm / Calibrated defocus min: 1.5 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Initial model |
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Refinement | Space: REAL / Protocol: RIGID BODY FIT | ||||||||||
Output model | PDB-7xxa: |