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Open data
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Basic information
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| Title | Structure of the Machupo virus glycoprotein complex | |||||||||||||||
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Keywords | Fusogen / glycoprotein / Complex / membrane / VIRAL PROTEIN | |||||||||||||||
| Function / homology | Function and homology informationhost cell Golgi membrane / receptor-mediated endocytosis of virus by host cell / host cell endoplasmic reticulum membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / metal ion binding / membrane Similarity search - Function | |||||||||||||||
| Biological species | Mammarenavirus machupoense | |||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||||||||
Authors | Mann CJ / Abraham J | |||||||||||||||
| Funding support | United States, 4 items
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Citation | Journal: Nat Microbiol / Year: 2025Title: Molecular organization of the New World arenavirus spike glycoprotein complex. Authors: Colin J Mann / Pan Yang / Daniel Olal / Xiaoyi Fan / Katherine Nabel Smith / Lars E Clark / Florian Krammer / Yuemin Bian / Jonathan Abraham / ![]() Abstract: Of the multiple arenaviruses that cause haemorrhagic fevers in the Americas, all lack reliable therapeutic options, and only one has a vaccine. The arenavirus glycoprotein complex (GPC) binds ...Of the multiple arenaviruses that cause haemorrhagic fevers in the Americas, all lack reliable therapeutic options, and only one has a vaccine. The arenavirus glycoprotein complex (GPC) binds cellular receptors and mediates pH-dependent fusion of viral and host cell membranes during entry. GPC comprises GP1, GP2 and stable signal peptide (SSP) subunits. SSP remains associated with the mature glycoprotein complex and regulates pH-dependent membrane fusion through an unclear mechanism. We report cryo-EM structures of Junin virus and Machupo virus GPC stabilized in the prefusion conformation using an amino acid substitution in the transmembrane region of SSP at 3.0 Å and 2.9 Å resolution, respectively. Mutational analyses, cell-cell fusion assays and molecular dynamics simulations reveal how contacts in the membrane-proximal and transmembrane regions of GPC regulate pH-dependent membrane fusion. The structures may aid in the design of therapeutic antibody cocktails, small-molecule inhibitors and vaccines against arenaviruses. | |||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_48598.map.gz | 373.4 MB | EMDB map data format | |
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| Header (meta data) | emd-48598-v30.xml emd-48598.xml | 24 KB 24 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_48598_fsc_1.xml emd_48598_fsc_2.xml | 17.9 KB 8.5 KB | Display Display | FSC data file |
| Images | emd_48598.png | 132.2 KB | ||
| Filedesc metadata | emd-48598.cif.gz | 6.5 KB | ||
| Others | emd_48598_additional_1.map.gz emd_48598_half_map_1.map.gz emd_48598_half_map_2.map.gz | 363.4 MB 391.2 MB 391.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-48598 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-48598 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9mt2MC ![]() 9mt6C M: atomic model generated by this map C: citing same article ( |
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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_48598.map.gz / Format: CCP4 / Size: 421.9 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: 0.73 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_48598_additional_1.map | ||||||||||||
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-Half map: #1
| File | emd_48598_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_48598_half_map_2.map | ||||||||||||
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Sample components
-Entire : Glycoprotein complex of Machupo virus
| Entire | Name: Glycoprotein complex of Machupo virus |
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| Components |
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-Supramolecule #1: Glycoprotein complex of Machupo virus
| Supramolecule | Name: Glycoprotein complex of Machupo virus / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1, #3 |
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| Source (natural) | Organism: Mammarenavirus machupoense / Strain: Carvallo |
-Macromolecule #1: Pre-glycoprotein polyprotein GP complex
| Macromolecule | Name: Pre-glycoprotein polyprotein GP complex / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mammarenavirus machupoense / Strain: Carvallo |
| Molecular weight | Theoretical: 6.351606 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MGQLISFFQE IPVFLQEALN IALVAVSLIA VIAGIINLYK SGLFQFIFFL LLAGRSCS UniProtKB: Pre-glycoprotein polyprotein GP complex |
-Macromolecule #2: Pre-glycoprotein polyprotein GP complex
| Macromolecule | Name: Pre-glycoprotein polyprotein GP complex / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mammarenavirus machupoense |
| Molecular weight | Theoretical: 23.528803 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: DGTFKIGLHT EFQSVTLTMQ RLLANHSNEL PSLCMLNNSF YYMRGGVNTF LIRVSDISVL MKEYDVSIYE PEDLGNCLNK SDSSWAIHW FSNALGHDWL MDPPMLCRNK TKKEGSNIQF NISKADDARV YGKKIRNGMR HLFRGFHDPC EEGKVCYLTI N QCGDPSSF ...String: DGTFKIGLHT EFQSVTLTMQ RLLANHSNEL PSLCMLNNSF YYMRGGVNTF LIRVSDISVL MKEYDVSIYE PEDLGNCLNK SDSSWAIHW FSNALGHDWL MDPPMLCRNK TKKEGSNIQF NISKADDARV YGKKIRNGMR HLFRGFHDPC EEGKVCYLTI N QCGDPSSF DYCGVNHLSK CQFDHVNTLH FLVRSKTHLN FERSLK UniProtKB: Pre-glycoprotein polyprotein GP complex |
-Macromolecule #3: Pre-glycoprotein polyprotein GP complex
| Macromolecule | Name: Pre-glycoprotein polyprotein GP complex / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Mammarenavirus machupoense |
| Molecular weight | Theoretical: 27.117402 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: AFFSWSLTDS SGKDMPGGYC LEEWMLIAAK MKCFGNTAVA KCNQNHDSEF CDMLRLFDYN KNAIKTLNDE AKKEINLLSQ AVNALISDN LLMKNKIKEL MSIPYCNYTK FWYVNHTLTG QHTLPRCWLI RNGSYLNTSE FRNDWILESD HLISEMLSKE Y AERQGKTP ...String: AFFSWSLTDS SGKDMPGGYC LEEWMLIAAK MKCFGNTAVA KCNQNHDSEF CDMLRLFDYN KNAIKTLNDE AKKEINLLSQ AVNALISDN LLMKNKIKEL MSIPYCNYTK FWYVNHTLTG QHTLPRCWLI RNGSYLNTSE FRNDWILESD HLISEMLSKE Y AERQGKTP ITLVDICFWS TIFFTASLFL HLVGIPTHRH LKGEACPLPH KLDSFGGCRC GKYPRLKKPT IWHKRH UniProtKB: Pre-glycoprotein polyprotein GP complex |
-Macromolecule #6: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 6 / Number of copies: 12 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-Macromolecule #7: ZINC ION
| Macromolecule | Name: ZINC ION / type: ligand / ID: 7 / Number of copies: 6 / Formula: ZN |
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| Molecular weight | Theoretical: 65.409 Da |
-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: FEI FALCON IV (4k x 4k) / Average electron dose: 53.43 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: 2.0 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Mammarenavirus machupoense
Authors
United States, 4 items
Citation




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












































Homo sapiens (human)
Processing
FIELD EMISSION GUN

