An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles.
Bottom Line: Heterologous sequences have been successfully inserted at both amino and carboxy termini as well as internally at the major immunodominant epitope.The insert was seen to form a trimeric spike on the capsid surface that was poorly resolved, most likely owing to it being flexible.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
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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.