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- EMDB-31248: recombinant Alfalfa Mosaic virus coat protein virus-like particle... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-31248 | |||||||||
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Title | recombinant Alfalfa Mosaic virus coat protein virus-like particle (rAMV-CP VLP) | |||||||||
![]() | Alfafa Mosaic virus-like protein T=1 | |||||||||
![]() | Alfalfa mosaic virus != Alfalfa mosaic virus (strain 425 / isolate Madison) Alfalfa mosaic virus
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![]() | alfalfa mosaic virus / virus-like particle / VIRUS LIKE PARTICLE | |||||||||
Function / homology | Coat protein, Ilarvirus / Ilarvirus coat protein / T=3 icosahedral viral capsid / translational initiation / viral nucleocapsid / RNA binding / Capsid protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.4 Å | |||||||||
![]() | Jeong H / Lee S | |||||||||
![]() | ![]() Title: Characterization of alfalfa mosaic virus capsid protein using Cryo-EM. Authors: Hyeongseop Jeong / Youngmin Park / Sooji Song / Kyungmin Min / Jae-Sung Woo / Young-Ho Lee / Eun-Ju Sohn / Sangmin Lee / ![]() Abstract: VLPs are virus-like particles that comprise viral capsid proteins that can self-assemble and mimic the shape and size of real viral particles; however, because they do not contain genetic material ...VLPs are virus-like particles that comprise viral capsid proteins that can self-assemble and mimic the shape and size of real viral particles; however, because they do not contain genetic material they cannot infect host cells. VLPs have great potential as safe drug/vehicle candidates; therefore, they are gaining popularity in the field of preventive medicine and therapeutics. Indeed, extensive studies are underway to examine their role as carriers for immunization and as vehicles for delivery of therapeutic agents. Here, we examined the possibility of developing VLP-utilizing technology based on an efficient VLP production process and high-resolution structural analysis. Nicotiana benthamiana was used as an expression platform to produce the coat protein of the alfalfa mosaic virus (AMV-CP). About 250 mg/kg of rAMV-CP was produced from Nicotiana benthamiana leaves. Structural analysis revealed that the oligomeric status of rAMV-CP changed according to the composition and pH of the buffer. Size exclusion chromatography and electron microscopy analysis confirmed the optimal conditions for rAMV-CP VLP formation, and a 2.4 Å resolution structure was confirmed by cryo-EM analysis. Based on the efficient protein production, VLP manufacturing technology, and high-resolution structure presented herein, we suggest that rAMV-CP VLP is a useful platform for development of various new drugs. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 482.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.4 KB 9.4 KB | Display Display | ![]() |
Images | ![]() | 90.6 KB | ||
Filedesc metadata | ![]() | 4.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7eppMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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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 | Alfafa Mosaic virus-like protein T=1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.865 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Alfalfa mosaic virus
Entire | Name: Alfalfa mosaic virus |
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Components |
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-Supramolecule #1: Alfalfa mosaic virus (strain 425 / isolate Madison)
Supramolecule | Name: Alfalfa mosaic virus (strain 425 / isolate Madison) / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1 / NCBI-ID: 12323 Sci species name: Alfalfa mosaic virus (strain 425 / isolate Madison) Virus type: VIRUS-LIKE PARTICLE / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes |
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-Macromolecule #1: Capsid protein
Macromolecule | Name: Capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 28.373334 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: CMQVWPPIGK KKFETLSYLP DLTGSMSSSQ KKAGGKAGKP TKRSQNYAAL RKAQLPKPPA LKVPVVKPTN TILPQTGCVW QSLGTPLSL SSFNGLGVRF LYSFLKDFAG PRILEEDLIY RMVFSITPSY AGTFCLTDDV TTEDGRAVAH GNPMQEFPHG A FHANEKFG ...String: CMQVWPPIGK KKFETLSYLP DLTGSMSSSQ KKAGGKAGKP TKRSQNYAAL RKAQLPKPPA LKVPVVKPTN TILPQTGCVW QSLGTPLSL SSFNGLGVRF LYSFLKDFAG PRILEEDLIY RMVFSITPSY AGTFCLTDDV TTEDGRAVAH GNPMQEFPHG A FHANEKFG FELVFTAPTH AGMQNQNFKH SYAVALCLDF DAQPEGSKNP SYRFNEVWVE RKAFPRAGPL RSLITVGLLD EA DDLDRHP RGHHHHHH UniProtKB: Capsid protein |
-Macromolecule #2: water
Macromolecule | Name: water / type: ligand / ID: 2 / Number of copies: 30 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-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: COUNTING / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 279755 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |