A VLP vaccine platform comprising the core protein of hepatitis B virus with N-terminal antigen capture.

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Tác giả: Kaniz Fatema, Neil A Ranson, David J Rowlands, Lee Sherry, Joseph S Snowden, Nicola J Stonehouse, Alexander Watson

Ngôn ngữ: eng

Ký hiệu phân loại:

Thông tin xuất bản: Netherlands : International journal of biological macromolecules , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 643030

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.
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