8UR7
I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-6heptad-I53_dn5 (local refinement of TH-6heptad)
Summary for 8UR7
| Entry DOI | 10.2210/pdb8ur7/pdb |
| EMDB information | 42486 |
| Descriptor | Trimer head HA,Hemagglutinin HA1 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | influenza virus, hemagglutinin nanoparticle vaccine, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein |
| Biological source | synthetic construct More |
| Total number of polymer chains | 3 |
| Total formula weight | 147732.61 |
| Authors | Park, Y.J.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2023-10-25, release date: 2023-12-27, Last modification date: 2024-10-23) |
| Primary citation | Ellis, D.,Dosey, A.,Boyoglu-Barnum, S.,Park, Y.J.,Gillespie, R.,Syeda, H.,Hutchinson, G.B.,Tsybovsky, Y.,Murphy, M.,Pettie, D.,Matheson, N.,Chan, S.,Ueda, G.,Fallas, J.A.,Carter, L.,Graham, B.S.,Veesler, D.,Kanekiyo, M.,King, N.P. Antigen spacing on protein nanoparticles influences antibody responses to vaccination. Cell Rep, 42:113552-113552, 2023 Cited by PubMed Abstract: Immunogen design approaches aim to control the specificity and quality of antibody responses elicited by next-generation vaccines. Here, we use computational protein design to generate a nanoparticle vaccine platform based on the receptor-binding domain (RBD) of influenza hemagglutinin (HA) that enables precise control of antigen conformation and spacing. HA RBDs are presented as either monomers or native-like closed trimers that are connected to the underlying nanoparticle by a rigid linker that is modularly extended to precisely control antigen spacing. Nanoparticle immunogens with decreased spacing between trimeric RBDs elicit antibodies with improved hemagglutination inhibition and neutralization potency as well as binding breadth across diverse H1 HAs. Our "trihead" nanoparticle immunogen platform provides insights into anti-HA immunity, establishes antigen spacing as an important parameter in structure-based vaccine design, and embodies several design features that could be used in next-generation vaccines against influenza and other viruses. PubMed: 38096058DOI: 10.1016/j.celrep.2023.113552 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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