ev d68 mo strain vlp (Databank Inc)
86
Structured Review
Databank Inc
ev d68 mo strain vlp
Ev D68 Mo Strain Vlp, supplied by Databank Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ev/d68+ev+mo+strain+vlp/pmc13264187-304-5-16
Average 86 stars, based on 1 article reviews
Ev D68 Mo Strain Vlp, supplied by Databank Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ev/d68+ev+mo+strain+vlp/pmc13264187-304-5-16
Average 86 stars, based on 1 article reviews
ev d68 mo strain vlp - by Bioz Stars,
2026-11
86/100 stars
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1) Product Images from "Comparative immunogenic and structural analysis of virus-like particle and inactivated whole-virion vaccines against enterovirus D68"
Article Title: Comparative immunogenic and structural analysis of virus-like particle and inactivated whole-virion vaccines against enterovirus D68
Journal: Molecular Therapy. Nucleic Acids
doi: 10.1016/j.omtn.2026.102957
Figure Legend Snippet: Preparation and characterization of IWV and VLP (A) Schematic representation of the construction of plasmids encoding EV-D68 P1 and 3CD. (B) Workflow for the expression and purification of VLP. (C–F) SDS-PAGE analysis of purified IWV and VLP. (C and D) VLP expressed in (C) Expi293F cells and (D) ExpiCHO-S cells purified with sucrose. The Hsp and Hsc identified by mass spectrometry are labeled in red lines. (E) VLP was expressed in ExpiCHO-S cells and further purified using both sucrose and iodixanol (OptiPrep) gradients. (F) IWV was purified by sucrose gradient ultracentrifugation. (G) IWV and VLP particle size distribution was measured by dynamic light scattering. (H) Representative negative-stain TEM images of IWV and VLP. Scale bars, 100 nm. (I) The thermal stability of the non-inactivated virus, IWV, and VLP was assessed using differential scanning fluorimetry (DSF). Data represent the mean of four independent measurements ( n = 4) for each sample.
Techniques Used: Expressing, Purification, SDS Page, Mass Spectrometry, Labeling, Staining, Virus
Figure Legend Snippet: Epitope specificities of IgG induced by IWV and VLP vaccines (A) Localization of neutralizing antigenic sites I–IV and corresponding epitope peptide sequences. Neutralizing antigenic sites I–IV were mapped onto a single icosahedral asymmetric unit of the EV-D68 MO strain capsid, based on the previously reported cryo-EM structure (PDB: 6CSG ). VP1, VP2, and VP3 are shown in gray, pink, and cyan, respectively. Neutralizing antigenic sites I, II, III, and IV are highlighted in yellow, green, blue, and magenta, respectively. The accompanying table lists the sequences of epitope peptides spanning the antigenic sites; residues constituting the neutralizing antigenic sites are indicated in red. Molecular graphics were generated using UCSF ChimeraX v1.9. (B) Plasma IgG levels specific to epitope peptides following boost immunization with either IWV or VLP. (C) Plasma IgG reactivity to mutant VLPs following boost immunization with IWV or wild-type VLP. Then, 1,000-fold diluted plasma samples were used. Details of the mutations in each mutant are summarized in the table on the right. (B–C) n = 5 per group. Data are presented as mean ± SD. (B) Statistical comparisons were performed using 50-fold diluted plasma samples. (B) “ns” indicates not significant. ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001, as determined by Tukey’s test. (C) ∗ p < 0.05 and ∗∗∗∗ p < 0.0001, as determined by Dunnett’s multiple comparison test.
Techniques Used: Vaccines, Cryo-EM Sample Prep, Generated, Clinical Proteomics, Mutagenesis, Comparison
Figure Legend Snippet: Cryo-EM structure of EV-D68 MO strain VLP (A) Cryo-EM density maps showing the overall structures of the mature virion (PDB: 6CSG ), empty particle (PDB: 6CRU ), and VLP of the EV-D68 MO strain. A schematic illustration of the viral particle is shown in the left-most. The 5-, 3-, and 2-fold symmetry axes are indicated by a pentagon, triangle, and circle, respectively. (B) Ribbon representations of the mature virion (PDB: 6CSG ), empty particle (PDB: 6CRU ), and VLP structures around the 2-fold axis. The 3-fold and 2-fold axes are denoted by a triangle and circle, respectively. (C) Structural comparison of the icosahedral asymmetric units of the VLP with those of the mature virion (left, PDB: 6CSG ) and the empty particle (middle, PDB: 6CRU ). VP1, VP0, and VP3 of the VLP were superimposed onto the corresponding subunits of the mature virion and the empty particle. Representative structures are shown based on superposition via VP1. All structures are depicted as ribbon models. The table on the right summarizes the number of pruned atom pairs and root-mean-square deviation (RMSD) values for each superposition.
Techniques Used: Cryo-EM Sample Prep, Comparison
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Electron Microscopy:Article Title: Comparative immunogenic and structural analysis of virus-like particle and inactivated whole-virion vaccines against enterovirus D68 Article Snippet: .. The cryo-EM map of the |
