VIRUS LIKE PARTICLE / P22 coat protein / designed protein
Function / homology
Major capsid protein Gp5 / P22 coat protein - gene protein 5 / viral procapsid / viral procapsid maturation / T=7 icosahedral viral capsid / viral capsid / identical protein binding / Major capsid protein
Function and homology information
Biological species
Lederbergvirus
Method
ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.02 Å
Journal: Adv Healthc Mater / Year: 2024 Title: A pH-Responsive Virus-Like Particle as a Protein Cage for a Targeted Delivery. Authors: Kwan-Jip Kim / Gijeong Kim / Jin-Ho Bae / Ji-Joon Song / Hak-Sung Kim / Abstract: A stimuli-responsive protein self-assembly offers promising utility as a protein nanocage for biotechnological and medical applications. Herein, the development of a virus-like particle (VLP) that ...A stimuli-responsive protein self-assembly offers promising utility as a protein nanocage for biotechnological and medical applications. Herein, the development of a virus-like particle (VLP) that undergoes a transition between assembly and disassembly under a neutral and acidic pH, respectively, for a targeted delivery is reported. The structure of the bacteriophage P22 coat protein is used for the computational design of coat subunits that self-assemble into a pH-responsive VLP. Subunit designs are generated through iterative computational cycles of histidine substitutions and evaluation of the interaction energies among the subunits under an acidic and neutral pH. The top subunit designs are tested and one that is assembled into a VLP showing the highest pH-dependent structural transition is selected. The cryo-EM structure of the VLP is determined, and the structural basis of a pH-triggered disassembly is delineated. The utility of the designed VLP is exemplified through the targeted delivery of a cytotoxic protein cargo into tumor cells in a pH-dependent manner. These results provide strategies for the development of self-assembling protein architectures with new functionality for diverse applications.
Conc.: 17 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen support
Details: The grid was glow discharged at 15 mA for 1 min. / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
Vitrification
Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 288 K
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Electron microscopy imaging
Microscopy
Model: TFS GLACIOS
Electron gun
Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: OTHER
Electron lens
Mode: BRIGHT FIELD / Nominal magnification: 92000 X / Nominal defocus max: 2800 nm / Nominal defocus min: 1200 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm
Image recording
Average exposure time: 52.69 sec. / Electron dose: 40 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 1654
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Processing
EM software
ID
Name
Category
Details
1
crYOLO
particleselection
4
RELION
CTFcorrection
7
UCSF Chimera
modelfitting
9
ISOLDE
modelrefinement
10
PHENIX
modelrefinement
14
PHENIX
3Dreconstruction
densitymodificationwascarriedoutatPHENIX
CTF correction
Type: PHASE FLIPPING ONLY
Particle selection
Num. of particles selected: 25282
3D reconstruction
Resolution: 4.02 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 3320 / Symmetry type: POINT
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