An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles.
Bottom Line: Virus-like particles composed of the core antigen of hepatitis B virus (HBcAg) have been shown to be an effective platform for the display of foreign epitopes in vaccine development.Heterologous sequences have been successfully inserted at both amino and carboxy termini as well as internally at the major immunodominant epitope.We hypothesise that the capacity of N-terminal inserts to form trimers may have application in the development of multivalent vaccines to trimeric antigens.
Affiliation: MRC-University of Glasgow Centre for Virus Research, Sir Michael Stoker Building, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, Scotland, UK.Show MeSH
Related in: MedlinePlus
Mentions: To confirm our findings, we evaluated local resolution within the maps using an alternative method: the Bsoft routine Blocres (Cardone et al., 2013). This approach calculates Fourier shell correlation values for a sliding box to yield a resolution map (Fig. 3). Supporting the results obtained with ResMap, Blocres determined that the T = 3 structure was resolved at between 6 and 9 Å within the HBcAg region while the N-terminal extension was estimated to be resolved at between 10 and 11 Å. The resolution estimates for the T = 4 VLP were also consistent with the ResMap output, measuring between 8 and 10 Å within the core components while the structure of the putative trimeric spike was solved at poorer than 14 Å resolution.
Affiliation: MRC-University of Glasgow Centre for Virus Research, Sir Michael Stoker Building, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, Scotland, UK.