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Instruments / Technical Area	Publication Details	Published	Actions
	Mammalian expression of virus-like particles as a proof of principle for next generation polio vaccines Mohammad W. Bahar , Claudine Porta , Helen Fox , Andrew J. Macadam , Elizabeth E. Fry , David I. Stuart Npj Vaccines 6 DOI: 10.1038/s41541-020-00267-3 Open Access Show Abstract ▼ Abstract: Global vaccination programs using live-attenuated oral and inactivated polio vaccine (OPV and IPV) have almost eradicated poliovirus (PV) but these vaccines or their production pose significant risk in a polio-free world. Recombinant PV virus-like particles (VLPs), lacking the viral genome, represent safe next-generation vaccines, however their production requires optimisation. Here we present an efficient mammalian expression strategy producing good yields of wild-type PV VLPs for all three serotypes and a thermostabilised variant for PV3. Whilst the wild-type VLPs were predominantly in the non-native C-antigenic form, the thermostabilised PV3 VLPs adopted the native D-antigenic conformation eliciting neutralising antibody titres equivalent to the current IPV and were indistinguishable from natural empty particles by cryo-electron microscopy with a similar stabilising lipidic pocket-factor in the VP1 β-barrel. This factor may not be available in alternative expression systems, which may require synthetic pocket-binding factors. VLPs equivalent to these mammalian expressed thermostabilized particles, represent safer non-infectious vaccine candidates for the post-eradication era.	Jan 2021
I03-Macromolecular Crystallography	Development of a structural epitope mimic: an idiotypic approach to HCV vaccine design Vanessa M. Cowton , Ania M. Owsianka , Valeria Fadda , Ana Maria Ortega-Prieto , Sarah J. Cole , Jane A. Potter , Jessica K. Skelton , Nathan Jeffrey , Caterina Di Lorenzo , Marcus Dorner , Garry L. Taylor , Arvind H. Patel Npj Vaccines 6 DOI: 10.1038/s41541-020-00269-1 Diamond Proposal Number(s): [10071] Open Access Show Abstract ▼ Abstract: HCV vaccine development is stymied by the high genetic diversity of the virus and the variability of the envelope glycoproteins. One strategy to overcome this is to identify conserved, functionally important regions—such as the epitopes of broadly neutralizing antibodies (bNAbs)—and use these as a basis for structure-based vaccine design. Here, we report an anti-idiotype approach that has generated an antibody that mimics a highly conserved neutralizing epitope on HCV E2. Crucially, a mutagenesis screen was used to identify the antibody, designated B2.1 A, whose binding characteristics to the bNAb AP33 closely resemble those of the original antigen. Protein crystallography confirmed that B2.1 A is a structural mimic of the AP33 epitope. When used as an immunogen B2.1 A induced antibodies that recognized the same epitope and E2 residues as AP33 and most importantly protected against HCV challenge in a mouse model.	Jan 2021

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