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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Beluga whale coronavirus spike glycoprotein | |||||||||
Map data | local resolution filtered map | |||||||||
Sample |
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Keywords | spike / glycoprotein / coronavirus / VIRAL PROTEIN | |||||||||
| Function / homology | Function and homology informationreceptor-mediated virion attachment to host cell / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion membrane / membrane Similarity search - Function | |||||||||
| Biological species | Beluga whale coronavirus SW1 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.24 Å | |||||||||
Authors | Hulswit RJG / Hurdiss DL | |||||||||
| Funding support | Switzerland, 1 items
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Citation | Journal: PLoS Pathog / Year: 2026Title: Cetacean coronavirus spikes highlight S glycoprotein structural plasticity. Authors: Ruben J G Hulswit / Tatiana M Shamorkina / Joline van der Lee / Floor Rosman / Lisanne S Wetzels / Frank J M van Kuppeveld / Joost Snijder / Berend Jan Bosch / Daniel L Hurdiss / ![]() Abstract: Coronaviruses (CoVs) exhibit a remarkable ability for spill-over infections into naive host populations. While much research has focused on the spike (S) glycoproteins of zoonotic alpha- and ...Coronaviruses (CoVs) exhibit a remarkable ability for spill-over infections into naive host populations. While much research has focused on the spike (S) glycoproteins of zoonotic alpha- and betacoronaviruses, the S proteins of gamma- and deltacoronaviruses, which predominantly infect avian hosts, remain poorly understood. Here, we present high-resolution cryo-EM structures of S proteins from two distinct gammacoronaviruses (75.7% sequence identity) that atypically infect marine mammals and belong to the Gammacoronavirus delphinapteri species. The cryo-EM reconstructions reveal that the spikes exhibit a unique quaternary architecture that distinguishes them from other coronaviruses. The S protein features a previously unidentified, tripodal quaternary assembly of the S1 subunit, in which S1B domains are presented in an upright position while their putative receptor binding sites are shielded by extended loops from the S1A domain of the same protomers. Additionally, the CeCoV spike proteins have evolved an additional and unique ~200 residue N-terminal domain (S10). S10 lacks homology to known protein sequences but displays structural similarity to members of the cupin protein superfamily. This represents a remarkable case of coronaviral exaptation of a host protein integrated into the S glycoprotein. Moreover, glycoproteomic analyses reveal that CeCoV S proteins are extensively N-glycosylated (>100 N-glycans per trimer), with a notable abundance of high-mannose glycans on S10 and O-glycosylation sites within a mucin-like loop at the trimer apex, all contributing to a dense glycan shield and potentially masking immunogenic epitopes. These findings demonstrate the structural diversity and adaptability of CoV S proteins, including alternative quaternary assemblies, additional domains, and diverse glycosylation strategies, offering new insights into the evolutionary mechanisms that enable coronaviruses to expand their host range and establish infections in novel species. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_53512.map.gz | 5.1 MB | EMDB map data format | |
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| Header (meta data) | emd-53512-v30.xml emd-53512.xml | 22.9 KB 22.9 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_53512_fsc.xml | 12.6 KB | Display | FSC data file |
| Images | emd_53512.png | 70.5 KB | ||
| Filedesc metadata | emd-53512.cif.gz | 7.4 KB | ||
| Others | emd_53512_additional_1.map.gz emd_53512_half_map_1.map.gz emd_53512_half_map_2.map.gz | 108.8 MB 200.4 MB 200.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53512 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53512 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9r1qMC ![]() 9r1rC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_53512.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | local resolution filtered map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.08854 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Unsharpened map
| File | emd_53512_additional_1.map | ||||||||||||
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| Annotation | Unsharpened map | ||||||||||||
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| Density Histograms |
-Half map: unfiltered half map A
| File | emd_53512_half_map_1.map | ||||||||||||
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| Annotation | unfiltered half map A | ||||||||||||
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| Density Histograms |
-Half map: unfiltered half map B
| File | emd_53512_half_map_2.map | ||||||||||||
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| Annotation | unfiltered half map B | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Beluga whale coronavirus spike glycoprotein
| Entire | Name: Beluga whale coronavirus spike glycoprotein |
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| Components |
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-Supramolecule #1: Beluga whale coronavirus spike glycoprotein
| Supramolecule | Name: Beluga whale coronavirus spike glycoprotein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Beluga whale coronavirus SW1 |
-Macromolecule #1: Spike protein
| Macromolecule | Name: Spike protein / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Beluga whale coronavirus SW1 |
| Molecular weight | Theoretical: 153.930609 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: IDEGLWPAGM WYSHLLQENN TYTVAAFQEH AILPSYVNNN WTVITNFTAE NATQLEWDDP YYNSTLFSYV NITMVGDNCI GNFTNRTLG ELGDIDYFPF NCTNVTNEFR TNYGYFIQNV MVARCLSSLC AVIIPKGRVF FEKNEMWWWS WQDRYQPGNY T FRHERFMS ...String: IDEGLWPAGM WYSHLLQENN TYTVAAFQEH AILPSYVNNN WTVITNFTAE NATQLEWDDP YYNSTLFSYV NITMVGDNCI GNFTNRTLG ELGDIDYFPF NCTNVTNEFR TNYGYFIQNV MVARCLSSLC AVIIPKGRVF FEKNEMWWWS WQDRYQPGNY T FRHERFMS LSQNITVIGL AGNFSLFGLG QTININSASY DWGTVIRGRL DDRICELQMT GADLCNLTRV DTSSDAFYTA GL VRPASAA LIADGAYKPI FTGVFHDNET HQVLYENATI KPSVRSFQVK NNDFDALYVG RKEKFSIDAV TIIFRLKETS TYL DLPFCN ETRVDKSDKA IIGYLIGGDF YSVDVSSIVI ERYNPPQPNA TSIPTTISTV STTTSGWEDL RSLNMSCVRF DYKL KKVMS VPLPMVKAFI IDFKQRQLAI DGFPVGALIA DFEFRFSIVA MPQTFISTLN YTTALVTFDK GNVRSVIDCN SEKPF DRLR CDLQTDVVSD GFYPVNIKTN EAKENTTFID VPATLANLTL EVFVSSPEQS PACVIKSYKC VDTRYFYISD YSYSCA ENG IPNDAAGAAY CRGVLDQINN YGVRGMDFKG KCPFAGSKVN SGLTFDKICF GVYEQGCQSD KACRFGFYFD NVQFSQY GN KLYYKPQDLG FIDYQFGTLF KNSLVQSNII QEGCHDYDIY GYKGTGVVKP FSDYSYLQTG GLIMLDSGGF PSLFRYNF A LYEVTQCTRE VAQLAVASNN AIGYYLPKQV TIDGVNASTS CNTTGAFKYC YYDDVIHVGR DVSNVTINVC NPSLMMENS HCINIQGNFM VNEPAITFNS TQYQPLLGVS GDVQLPRTLM LHTTTEFIQT HSPKIVIDCT KYVCGSSERC RRILVKYGGF CESIMRLLN GVNMADDVSV TDFLDNFNSF DNISVSLQNL NASFGQFEGY GFQKFLPKSF DFDGSDPRDA RSTIEDILFD K VTTVGLGT VDADYDKCTK GLSVADLVCA QYYNGIMVLP GVADAEKMAM YTGALVGGMV LGGITSAAAI PFATQIQARV NY LALTQNA IQENQKIIVQ QFNKAIDSMT SAFQSVNEGF SAVSSAITEV QNAVNAQSQA LTKLLGQLNY NFGATTSSIK ELY ERLAPP EADVQVDRLI NGRLTALSAF VAARQVEAAK VASQRVLAAE KINECVKSTS NRYGFCGNGA HIISFPQNAP NGML FVHFS LVPNETITVK GIIGLCLNNS IGIVPAKDRG MFIQCSNGTY CPEFENSFNE SKNGNVTFPF AITSREQYNP RQITT GDIQ MLTSCNSGYT HIEWSQLPLV APPYDDFDKE FDKLYEKWNY TLEELEKLNV TFPYLNVSEQ IDIINSAMEN IKSQIQ NLN SSYIDLEWLN KYER UniProtKB: Spike protein |
-Macromolecule #12: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 12 / Number of copies: 30 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 105000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Beluga whale coronavirus SW1
Authors
Switzerland, 1 items
Citation



Z (Sec.)
Y (Row.)
X (Col.)












































Homo sapiens (human)
Processing
FIELD EMISSION GUN

