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
Related in: MedlinePlus
Mentions: Resmap analysis (Kucukelbir et al., 2014) of the T = 3 reconstruction indicated a mean resolution of 7.8 Å; significantly better than the estimate derived by the FSC0.5 method. Analysis of the T = 4 structure also indicated a better resolution than that estimated by Fourier shell correlation at 0.5 cutoff, the mean resolution was determined to be 10.6 Å (Fig. 2). Local resolution measurements were seen to range between 5 and 8 Å within the core regions of the T = 3 VLP, while in the T = 4 structure the HBcAg components were resolved at between 8 and 10 Å. Interestingly in both analyses the novel density that we attribute to the N-terminal extension was highlighted as having a substantially lower resolution than the HBcAg structure. For the T = 3 particle this region was determined to have a resolution poorer than 19 Å, likewise in the T = 4 structure the trimeric spike was identified as a region of low resolution.
Affiliation: MRC-University of Glasgow Centre for Virus Research, Sir Michael Stoker Building, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, Scotland, UK.