Design strategies to address the effect of hydrophobic epitope on stability and in vitro assembly of modular virus-like particle.

ABSTRACT: Virus-like particles (VLPs) and capsomere subunits have shown promising potential as safe and effective vaccine candidates. They can serve as platforms for the display of foreign epitopes on their surfaces in a modular architecture. Depending on the physicochemical properties of the antigenic modules, modularization may affect the expression, solubility and stability of capsomeres, and VLP assembly. In this study, three module designs of a rotavirus hydrophobic peptide (RV10) were synthesized using synthetic biology. Among the three synthetic modules, modularization of the murine polyomavirus VP1 with a single copy of RV10 flanked by long linkers and charged residues resulted in the expression of stable modular capsomeres. Further employing the approach of module titration of RV10 modules

SUBMITTER: Tekewe A 

PROVIDER: S-EPMC4972206 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature