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Yorodumi- EMDB-62810: Cryo-EM structure of SARS-CoV-2 S-BQ.1 in complex with ACE2 const... -
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Basic information
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| Title | Cryo-EM structure of SARS-CoV-2 S-BQ.1 in complex with ACE2 constituent map 2 | |||||||||
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Sample |
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Keywords | spike protein / VIRAL PROTEIN | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / Resolution: 3.2 Å | |||||||||
Authors | Hsu HF / Wu MH / Chang YC / Hsu STD | |||||||||
| Funding support | Taiwan, 2 items
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Citation | Journal: JCI Insight / Year: 2024Title: Functional and structural investigation of a broadly neutralizing SARS-CoV-2 antibody. Authors: Yi-Hsuan Chang / Min-Feng Hsu / Wei-Nan Chen / Min-Hao Wu / Wye-Lup Kong / Mei-Yeh Jade Lu / Chih-Heng Huang / Fang-Ju Chang / Lan-Yi Chang / Ho-Yang Tsai / Chao-Ping Tung / Jou-Hui Yu / ...Authors: Yi-Hsuan Chang / Min-Feng Hsu / Wei-Nan Chen / Min-Hao Wu / Wye-Lup Kong / Mei-Yeh Jade Lu / Chih-Heng Huang / Fang-Ju Chang / Lan-Yi Chang / Ho-Yang Tsai / Chao-Ping Tung / Jou-Hui Yu / Yali Kuo / Yu-Chi Chou / Li-Yang Bai / Yuan-Chih Chang / An-Yu Chen / Cheng-Cheung Chen / Yi-Hua Chen / Chun-Che Liao / Chih-Shin Chang / Jian-Jong Liang / Yi-Ling Lin / Takashi Angata / Shang-Te Danny Hsu / Kuo-I Lin / ![]() Abstract: Since its emergence, SARS-CoV-2 has been continuously evolving, hampering the effectiveness of current vaccines against COVID-19. mAbs can be used to treat patients at risk of severe COVID-19. Thus, ...Since its emergence, SARS-CoV-2 has been continuously evolving, hampering the effectiveness of current vaccines against COVID-19. mAbs can be used to treat patients at risk of severe COVID-19. Thus, the development of broadly protective mAbs and an understanding of the underlying protective mechanisms are of great importance. Here, we isolated mAbs from donors with breakthrough infection with Omicron subvariants using a single-B cell screening platform. We identified a mAb, O5C2, which possesses broad-spectrum neutralization and antibody-dependent cell-mediated cytotoxic activities against SARS-CoV-2 variants, including EG.5.1. Single-particle analysis by cryo-electron microscopy revealed that O5C2 targeted an unusually large epitope within the receptor-binding domain of spike protein that overlapped with the angiotensin-converting enzyme 2 binding interface. Furthermore, O5C2 effectively protected against BA.5 Omicron infection in vivo by mediating changes in transcriptomes enriched in genes involved in apoptosis and interferon responses. Our findings provide insights into the development of pan-protective mAbs against SARS-CoV-2. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_62810.map.gz | 186.4 MB | EMDB map data format | |
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| Header (meta data) | emd-62810-v30.xml emd-62810.xml | 14.9 KB 14.9 KB | Display Display | EMDB header |
| Images | emd_62810.png | 69.6 KB | ||
| Filedesc metadata | emd-62810.cif.gz | 5.1 KB | ||
| Others | emd_62810_half_map_1.map.gz emd_62810_half_map_2.map.gz | 344.8 MB 344.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-62810 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-62810 | HTTPS FTP |
-Validation report
| Summary document | emd_62810_validation.pdf.gz | 696.1 KB | Display | EMDB validaton report |
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| Full document | emd_62810_full_validation.pdf.gz | 695.6 KB | Display | |
| Data in XML | emd_62810_validation.xml.gz | 17 KB | Display | |
| Data in CIF | emd_62810_validation.cif.gz | 20.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-62810 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-62810 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_62810.map.gz / Format: CCP4 / Size: 371.3 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: 1.08 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_62810_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_62810_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : SARS-CoV-2 S-BQ.1 and ACE2 complex
| Entire | Name: SARS-CoV-2 S-BQ.1 and ACE2 complex |
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| Components |
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-Supramolecule #1: SARS-CoV-2 S-BQ.1 and ACE2 complex
| Supramolecule | Name: SARS-CoV-2 S-BQ.1 and ACE2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Spike glycoprotein
| Macromolecule | Name: Spike glycoprotein / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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| Sequence | String: MFVFLVLLPL VSSQCVNLIT RTQSYTNSFT RGVYYPDKVF RSSVLHSTQD LFLPFFSNVT WFHAISGTNG TKRFDNPVLP FNDGVYFAST EKSNIIRGWI FGTTLDSKTQ SLLIVNNATN VVIKVCEFQF CNDPFLDVYY HKNNKSWMES EFRVYSSANN CTFEYVSQPF ...String: MFVFLVLLPL VSSQCVNLIT RTQSYTNSFT RGVYYPDKVF RSSVLHSTQD LFLPFFSNVT WFHAISGTNG TKRFDNPVLP FNDGVYFAST EKSNIIRGWI FGTTLDSKTQ SLLIVNNATN VVIKVCEFQF CNDPFLDVYY HKNNKSWMES EFRVYSSANN CTFEYVSQPF LMDLEGKQGN FKNLREFVFK NIDGYFKIYS KHTPINLGRD LPQGFSALEP LVDLPIGINI TRFQTLLALH RSYLTPGDSS SGWTAGAAAY YVGYLQPRTF LLKYNENGTI TDAVDCALDP LSETKCTLKS FTVEKGIYQT SNFRVQPTES IVRFPNITNL CPFDEVFNAT RFASVYAWNR KRISNCVADY SVLYNFAPFF AFKCYGVSPT KLNDLCFTNV YADSFVIRGN EVSQIAPGQT GNIADYNYKL PDDFTGCVIA WNSNKLDSTV GGNYNYRYRL FRKSKLKPFE RDISTEIYQA GNKPCNGVAG VNCYFPLQSY GFRPTYGVGH QPYRVVVLSF ELLHAPATVC GPKKSTNLVK NKCVNFNFNG LTGTGVLTES NKKFLPFQQF GRDIADTTDA VRDPQTLEIL DITPCSFGGV SVITPGTNTS NQVAVLYQGV NCTEVPVAIH ADQLTPTWRV YSTGSNVFQT RAGCLIGAEY VNNSYECDIP IGAGICASYQ TQTKSHGSAS SVASQSIIAY TMSLGAENSV AYSNNSIAIP TNFTISVTTE ILPVSMTKTS VDCTMYICGD STECSNLLLQ YGSFCTQLKR ALTGIAVEQD KNTQEVFAQV KQIYKTPPIK YFGGFNFSQI LPDPSKPSKR SPIEDLLFNK VTLADAGFIK QYGDCLGDIA ARDLICAQKF KGLTVLPPLL TDEMIAQYTS ALLAGTITSG WTFGAGPALQ IPFPMQMAYR FNGIGVTQNV LYENQKLIAN QFNSAIGKIQ DSLSSTPSAL GKLQDVVNHN AQALNTLVKQ LSSKFGAISS VLNDILSRLD PPEAEVQIDR LITGRLQSLQ TYVTQQLIRA AEIRASANLA ATKMSECVLG QSKRVDFCGK GYHLMSFPQS APHGVVFLHV TYVPAQEKNF TTAPAICHDG KAHFPREGVF VSNGTHWFVT QRNFYEPQII TTDNTFVSGN CDVVIGIVNN TVYDPLQPEL DSFKEELDKY FKNHTSPDVD LGDISGINAS VVNIQKEIDR LNEVAKNLNE SLIDLQELGK YEQEFGSGGY IPEAPRDGQA YVRKDGEWVL LSTFLKGQDN SADIQHSGRP LESRGPFEQK LISEEDLNMH TGHHHHHH |
-Experimental details
-Structure determination
Processing | single particle reconstruction |
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| Aggregation state | 3D array |
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Sample preparation
| Concentration | 2 mg/mL |
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| Buffer | pH: 7.4 |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (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: 2.6 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: RIGID BODY FIT |
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Keywords
Authors
Taiwan, 2 items
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FIELD EMISSION GUN

