Evaluation of lumazine synthase from Bacillus anthracis as a presentation platform for polyvalent antigen display.

ABSTRACT: Polyvalent antigen display is an effective strategy to enhance the immunogenicity of subunit vaccines by clustering them in an array-like manner on a scaffold system. This strategy results in a higher local density of antigens, increased high avidity interactions with B cells and other antigen presenting cells, and therefore a more effective presentation of vaccine antigens. In this study, we used lumazine synthase (LS), an icosahedral symmetry capsid derived from Bacillus anthracis, as a scaffold to present 60 copies of a linear B cell epitope (PB10) from the ricin toxin fused to the C terminus of LS via four different linkers. We then investigated the effects of linker length, linker rigidity and formaldehyde crosslinking on the protein assembly, conformational integrity, thermal stabili

SUBMITTER: Wei Y 

PROVIDER: S-EPMC5606532 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature