Production and characterisation of dimeric spike Truncated-nodavirus capsid displaying the Receptor- binding domain of severe acute respiratory syndrome Coronavirus-2

Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a novel coronavirus (CoV) of zoonotic origin and is the causative agent for Coronavirus Disease 2019 (COVID-19), a pandemic that has claimed more than 6.9 million lives worldwide as of August 2023. Although antiviral drugs are available, vaccination remains the most effective measure to control the widespread of the virus. Since the declaration of COVID-19 as a pandemic in March 2020, several vaccines developed based on mRNA technology, attenuated whole virus, protein subunits and adeno-viral vector have been approved for emergency use. However, there are serious concerns over the safety and efficacy of these vaccines in preventing SARS-CoV-2 infections. Moreover, the cost and advanced technologies required for the production and storage of these vaccines have limited the global vaccination rate especially in poorer countries. Therefore, there is an urgent need to develop a safe, effective, and affordable vaccine for the prevention of SARS-CoV-2 infection. In this study, a vaccine candidate was developed by displaying the receptor-binding domain (RBD) of SARS-CoV-2 on the virus-like particle (VLP) derived from Macrobrachium rosenbergii nodavirus capsid protein (MrNV-CP). The RBD of the ancestral SARS-CoV-2 Wuhan strain was fused to the C-terminal region of the protruding (P) domain truncated-MrNV-CP (C116- MrNV-CP) to form the recombinant protein C-116-MrNV-CPRBD. The recombinant protein was expressed by Escherichia coli (E. coli) and purified with cation ion-exchange chromatography. Scanning transmission electron microscopic (STEM) analysis showed that C-116-MrNV-CPRBD self-assembled to form VLPs with a diameter of approximately 14 nm. Antigenicity assay showed that the fused RBD was exposed on the surface of the VLPs as it can be detected by anti-RBD monoclonal antibody. To demonstrate the immunogenicity of CΔ116-MrNV-CPRBD, BALB/c mice were immunised with the recombinant protein in the presence or absence of AddaVax as an adjuvant. Regardless of the presence of adjuvant, BALB/c mice immunised subcutaneously with CΔ116-MrNV-CPRBD exhibited both cellular and humoral immune responses. In conclusion, this study demonstrated the potential of C-116- MrNV-CP to serve as a robust platform for the development of VLP-based vaccines.

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