9FWE
N-VelcroVax HBcAg with SUMO-Affimer inserted at N-terminus (T=3 VLP)
Summary for 9FWE
| Entry DOI | 10.2210/pdb9fwe/pdb |
| EMDB information | 50832 |
| Descriptor | N-VelcroVax HBcAg with SUMO-Affimer inserted at N-terminus (1 entity in total) |
| Functional Keywords | velcrovax, hepatitis b virus, hepatitis b core antigen, affimer, vaccine, recombinant, vlp, antigen display, virus like particle |
| Biological source | synthetic construct |
| Total number of polymer chains | 3 |
| Total formula weight | 102515.93 |
| Authors | Fatema, K.,Snowden, J.S.,Watson, A.,Sherry, L.,Ranson, N.A.,Stonehouse, N.J.,Rowlands, D.J. (deposition date: 2024-06-30, release date: 2025-02-26, Last modification date: 2025-03-05) |
| Primary citation | Fatema, K.,Snowden, J.S.,Watson, A.,Sherry, L.,Ranson, N.A.,Stonehouse, N.J.,Rowlands, D.J. A VLP vaccine platform comprising the core protein of hepatitis B virus with N-terminal antigen capture. Int.J.Biol.Macromol., 305:141152-141152, 2025 Cited by PubMed Abstract: Nanoparticle presentation systems offer the potential to develop new vaccines rapidly in response to emerging diseases, a public health need that has become increasingly evident in the wake of the COVID-19 pandemic. Previously, we reported a nanoparticle scaffold system termed VelcroVax. This was constructed by insertion of a high affinity SUMO binding protein (Affimer), able to recognise a SUMO peptide tag, into the major immunodominant region of VLPs assembled from a tandem (fused dimer) form of hepatitis B virus (HBV) core protein (HBc). Here we describe an alternative form, termed N-VelcroVax, a VLP vaccine platform assembled from a monomeric HBc protein (N-anti-SUMO Affimer HBc 190) with the Affimer inserted at the N-terminus. In contrast to the tandem form of VelcroVax, N-VelcroVax VLPs were expressed well in E. coli. The VLPs effectively bound SUMO-tagged Junín virus glycoprotein, gp1 as assessed by structural and serological analyses. Cryo-EM characterisation of N-VelcroVax complexed with a SUMO-Junín gp1 showed continuous density attributable to the fused Affimer, in addition to evidence of target antigen capture. Collectively, these data suggest that N-VelcroVax has potential as a versatile next generation vaccine scaffold. PubMed: 39961558DOI: 10.1016/j.ijbiomac.2025.141152 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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