6HCR
Synthetic Self-assembling ADDomer Platform for Highly Efficient Vaccination by Genetically-encoded Multi-epitope Display
This is a non-PDB format compatible entry.
Summary for 6HCR
| Entry DOI | 10.2210/pdb6hcr/pdb |
| EMDB information | 0198 |
| Descriptor | Penton protein (1 entity in total) |
| Functional Keywords | engineered, virus, like, particle, addomer, ad3, penton, base, adenovirus, synthetic, vaccine, biobrick, human, homosapien, dodecahedron, icosohedral, epitode, display, scaffold, virus like particle |
| Biological source | Human adenovirus B serotype 3 |
| Total number of polymer chains | 60 |
| Total formula weight | 3815897.58 |
| Authors | Bufton, J.C.,Berger, I.,Schaffitzel, C.,Garzoni, F.,Rabi, F.A. (deposition date: 2018-08-16, release date: 2019-08-28, Last modification date: 2024-05-15) |
| Primary citation | Vragniau, C.,Bufton, J.C.,Garzoni, F.,Stermann, E.,Rabi, F.,Terrat, C.,Guidetti, M.,Josserand, V.,Williams, M.,Woods, C.J.,Viedma, G.,Bates, P.,Verrier, B.,Chaperot, L.,Schaffitzel, C.,Berger, I.,Fender, P. Synthetic self-assembling ADDomer platform for highly efficient vaccination by genetically encoded multiepitope display. Sci Adv, 5:eaaw2853-eaaw2853, 2019 Cited by PubMed Abstract: Self-assembling virus-like particles represent highly attractive tools for developing next-generation vaccines and protein therapeutics. We created ADDomer, an adenovirus-derived multimeric protein-based self-assembling nanoparticle scaffold engineered to facilitate plug-and-play display of multiple immunogenic epitopes from pathogens. We used cryo-electron microscopy at near-atomic resolution and implemented novel, cost-effective, high-performance cloud computing to reveal architectural features in unprecedented detail. We analyzed ADDomer interaction with components of the immune system and developed a promising first-in-kind ADDomer-based vaccine candidate to combat emerging Chikungunya infectious disease, exemplifying the potential of our approach. PubMed: 31620562DOI: 10.1126/sciadv.aaw2853 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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