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Open data
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Basic information
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Title | Infectious B19V capsid | |||||||||
![]() | A deepEMhancer-processed map of B19V-ITIH4 complex | |||||||||
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![]() | B19 / Virion / Capsid / VIRAL PROTEIN | |||||||||
Function / homology | ![]() hyaluronan metabolic process / platelet dense granule lumen / endopeptidase inhibitor activity / T=1 icosahedral viral capsid / response to cytokine / acute-phase response / serine-type endopeptidase inhibitor activity / Platelet degranulation / : / blood microparticle ...hyaluronan metabolic process / platelet dense granule lumen / endopeptidase inhibitor activity / T=1 icosahedral viral capsid / response to cytokine / acute-phase response / serine-type endopeptidase inhibitor activity / Platelet degranulation / : / blood microparticle / structural molecule activity / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
![]() | Lee H / Hafenstein S | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Infectious parvovirus B19 circulates in the blood coated with active host protease inhibitors. Authors: Hyunwook Lee / Ruben Assaraf / Suriyasri Subramanian / Dan Goetschius / Jan Bieri / Nadia M DiNunno / Remo Leisi / Carol M Bator / Susan L Hafenstein / Carlos Ros / ![]() ![]() Abstract: The lack of a permissive cell culture system has limited high-resolution structures of parvovirus B19 (B19V) to virus-like particles (VLPs). In this study, we present the atomic resolution structure ...The lack of a permissive cell culture system has limited high-resolution structures of parvovirus B19 (B19V) to virus-like particles (VLPs). In this study, we present the atomic resolution structure (2.2 Å) of authentic B19V purified from a patient blood sample. There are significant differences compared to non-infectious VLPs. Most strikingly, two host protease inhibitors (PIs), inter-alpha-trypsin inhibitor heavy chain 4 (ITIH4) and serpinA3, were identified in complex with the capsids in all patient samples tested. The ITIH4 binds specifically to the icosahedral fivefold axis and serpinA3 occupies the twofold axis. The protein-coated virions remain infectious, and the capsid-associated PIs retain activity; however, upon virion interaction with target cells, the PIs dissociate from the capsid prior to viral entry. Our finding of an infectious virion shielded by bound host serum proteins suggests an evolutionarily favored phenomenon to evade immune surveillance and escape host protease activity. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 451.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.7 KB 18.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 18 KB | Display | ![]() |
Images | ![]() | 142.7 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() ![]() | 480.2 MB 411.3 MB 411.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9c4fMC ![]() 9c27C ![]() 9c2tC ![]() 9c4nC ![]() 9d7kC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | A deepEMhancer-processed map of B19V-ITIH4 complex | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: B-factor sharpened map of B19V-ITIH4 complex
File | emd_45184_additional_1.map | ||||||||||||
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Annotation | B-factor sharpened map of B19V-ITIH4 complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: A half map-1 of B19V-ITIH4 complex
File | emd_45184_half_map_1.map | ||||||||||||
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Annotation | A half map-1 of B19V-ITIH4 complex | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: A half map-1 of B19V-ITIH4 complex
File | emd_45184_half_map_2.map | ||||||||||||
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Annotation | A half map-1 of B19V-ITIH4 complex | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Human parvovirus B19 with inter-alpha-trypsin inhibitor heavy chain H4
Entire | Name: Human parvovirus B19 with inter-alpha-trypsin inhibitor heavy chain H4 |
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Components |
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-Supramolecule #1: Human parvovirus B19 with inter-alpha-trypsin inhibitor heavy chain H4
Supramolecule | Name: Human parvovirus B19 with inter-alpha-trypsin inhibitor heavy chain H4 type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #3: Inter-alpha-trypsin inhibitor heavy chain H4
Supramolecule | Name: Inter-alpha-trypsin inhibitor heavy chain H4 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: ![]() |
-Supramolecule #2: Human parvovirus B19
Supramolecule | Name: Human parvovirus B19 / type: virus / ID: 2 / Parent: 1 / Macromolecule list: #1 / NCBI-ID: 10798 / Sci species name: Human parvovirus B19 / Virus type: VIRION / Virus isolate: SEROTYPE / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: Capsid protein 2
Macromolecule | Name: Capsid protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 60.916016 KDa |
Sequence | String: MTSVNSAEAS TGAGGGGSNP VKSMWSEGAT FSANSVTCTF SRQFLIPYDP EHHYKVFSPA ASSCHNASGK EAKVCTISPI MGYSTPWRY LDFNALNLFF SPLEFQHLIE NYGSIAPDAL TVTISEIAVK DVTDKTGGGV QVTDSTTGRL CMLVDHEYKY P YVLGQGQD ...String: MTSVNSAEAS TGAGGGGSNP VKSMWSEGAT FSANSVTCTF SRQFLIPYDP EHHYKVFSPA ASSCHNASGK EAKVCTISPI MGYSTPWRY LDFNALNLFF SPLEFQHLIE NYGSIAPDAL TVTISEIAVK DVTDKTGGGV QVTDSTTGRL CMLVDHEYKY P YVLGQGQD TLAPELPIWV YFPPQYAYLT VGDVNTQGIS GDSKKLASEE SAFYVLEHSS FQLLGTGGTA TMSYKFPPVP PE NLEGCSQ HFYEMYNPLY GSRLGVPDTL GGDPKFRSLT HEDHAIQPQN FMPGPLVNSV STKEGDSSNT GAGKALTGLS TGT SQNTRI SLRPGPVSQP YHHWDTDKYV TGINAISHGQ TTYGNAEDKE YQQGVGRFPN EKEQLKQLQG LNMHTYFPNK GTQQ YTDQI ERPLMVGSVW NRRALHYESQ LWSKIPNLDD SFKTQFAALG GWGLHQPPPQ IFLKILPQSG PIGGIKSMGI TTLVQ YAVG IMTVTMTFKL GPRKATGRWN PQPGVYPPHA AGHLPYVLYD PTATDAKQHH RHGYEKPEEL WTAKSRVHPL UniProtKB: Capsid protein 2 |
-Macromolecule #2: Inter-alpha-trypsin inhibitor heavy chain H4
Macromolecule | Name: Inter-alpha-trypsin inhibitor heavy chain H4 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 103.47025 KDa |
Sequence | String: MKPPRPVRTC SKVLVLLSLL AIHQTTTAEK NGIDIYSLTV DSRVSSRFAH TVVTSRVVNR ANTVQEATFQ MELPKKAFIT NFSMIIDGM TYPGIIKEKA EAQAQYSAAV AKGKSAGLVK ATGRNMEQFQ VSVSVAPNAK ITFELVYEEL LKRRLGVYEL L LKVRPQQL ...String: MKPPRPVRTC SKVLVLLSLL AIHQTTTAEK NGIDIYSLTV DSRVSSRFAH TVVTSRVVNR ANTVQEATFQ MELPKKAFIT NFSMIIDGM TYPGIIKEKA EAQAQYSAAV AKGKSAGLVK ATGRNMEQFQ VSVSVAPNAK ITFELVYEEL LKRRLGVYEL L LKVRPQQL VKHLQMDIHI FEPQGISFLE TESTFMTNQL VDALTTWQNK TKAHIRFKPT LSQQQKSPEQ QETVLDGNLI IR YDVDRAI SGGSIQIENG YFVHYFAPEG LTTMPKNVVF VIDKSGSMSG RKIQQTREAL IKILDDLSPR DQFNLIVFST EAT QWRPSL VPASAENVNK ARSFAAGIQA LGGTNINDAM LMAVQLLDSS NQEERLPEGS VSLIILLTDG DPTVGETNPR SIQN NVREA VSGRYSLFCL GFGFDVSYAF LEKLALDNGG LARRIHEDSD SALQLQDFYQ EVANPLLTAV TFEYPSNAVE EVTQN NFRL LFKGSEMVVA GKLQDRGPDV LTATVSGKLP TQNITFQTES SVAEQEAEFQ SPKYIFHNFM ERLWAYLTIQ QLLEQT VSA SDADQQALRN QALNLSLAYS FVTPLTSMVV TKPDDQEQSQ VAEKPMEGES RNRNVHSGST FFKYYLQGAK IPKPEAS FS PRRGWNRQAG AAGSRMNFRP GVLSSRQLGL PGPPDVPDHA AYHPFRRLAI LPASAPPATS NPDPAVSRVM NMKIEETT M TTQTPAPIQA PSAILPLPGQ SVERLCVDPR HRQGPVNLLS DPEQGVEVTG QYEREKAGFS WIEVTFKNPL VWVHASPEH VVVTRNRRSS AYKWKETLFS VMPGLKMTMD KTGLLLLSDP DKVTIGLLFW DGRGEGLRLL LRDTDRFSSH VGGTLGQFYQ EVLWGSPAA SDDGRRTLRV QGNDHSATRE RRLDYQEGPP GVEISCWSVE L UniProtKB: Inter-alpha-trypsin inhibitor heavy chain H4 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 100.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |