There is a need to develop a range different VLP for use as nanoscale templates and vaccines. The aim of this research was to develop RHDV VLP as a versatile vaccine delivery system easily modified for use against a wide range of different diseases. Production of Rabbit haemorrhagic disease virus (RHDV) capsid protein in a baculovirus system led to the self-assembly of Virus-like Particles (VLP) that could be purified to greater than 99% purity using simple methods. The capsid gene, vp60, can be manipulated genetically to incorporate immunogenic peptide sequences or a functional DNA-binding site. Fusion of these small epitopes to VP60 was well tolerated, forming VLP and greatly enhanced the presentation of peptide to, and activation of CD4+ T helper cell hybridoma. To avoid constraints imposed on chimeric VLP and dramatically increase the versatility of RHDV VLP, rapid conjugation of antigen was carried out, employing the hetero-bifunctional chemical linker, sulpho-SMCC. Incorporation of sulfhydral groups by design or treatment with SATA allowed for great versatility, in turn enabling many diverse peptides and proteins to be conjugated to VLP. RHDV VLP and consequently the conjugated GFP antigen were efficiently taken up by DC with more than 85% of DC positive for GFP by flow cytometry. This was also visualised by confocal microscopy and electron microscopy of both gold- labelled VLP and conjugated antigen. RHDV VLP conjugate was shown to induce the significant up regulation of the activation markers CD40, CD80, CD86 and MHC class II on the surface of dendritic cells (DC). As well, DC pulsed with RHDV VLP/OVA effectively presented OVA to both CD4+ and CD8+ T cells transgenic for respective peptide-specific T cell receptors, eliciting a greater proliferative response in both T cell subsets than antigen delivered alone. The surface accessibility of peptides on VLP was demonstrated, while administration of VLP/Ovalbumin (OVA) conjugate in mice was shown to evoke very high titre antibody responses specific for conjugated antigen. VLP/OVA conjugates were also shown to induce IFN-γ production and OVA-specific cytotoxic killing in vivo, of up to 80% of fluorescently labelled, adoptively transferred target cells. No distinguishable cytotoxicity was detected in unimmunised control mice. This assay was also used to demonstrate the necessity for antigen to be conjugated to VLP, as antigen mixed with VLP induced only sub-optimal killing. To investigate the anti-tumour effects, mice vaccinated with VLP conjugated to OVA protein, CD4+ or CD8+ T cell OVA epitopes were inoculated with B16- OVA tumour cells and monitored for tumour growth. Untreated control mice had to be sacrificed by day 19, while mice immunised with either VLP/OVA or VLP conjugated with both CD4+ and CD8+ OVA epitopes, showed a significant delay in tumour growth (P = 0.0002), with one mouse remaining free of palpable tumour until day 92. These results show that RHDV VLP can be easily produced and purified and demonstrate the versatility of this RHDV capsid. Rapid conjugation techniques allowed the modification of VLP with both peptide and protein rendered these antigens highly immunogenic, stimulating both humoral and cell-mediated immunity targeted against conjugated antigens of choice. The versatility and immune stimulating properties of RHDV VLP provides a molecular tool with almost limitless applications within the fields of nanotechnology and immunology.