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A novel expression system based on engineered variants of the yeast ( Saccharomyces cerevisiae ) dsRNA virus L-A was developed allowing the  in vivo  assembly of chimeric virus-like particles (VLPs) as a unique platform for a wide range of applications. We show that polypeptides fused to the viral capsid protein Gag self-assemble into isometric VLP chimeras carrying their cargo inside the capsid, thereby not only effectively preventing proteolytic degradation in the host cell cytosol, but also allowing the expression of a  per se  cytotoxic protein. Carboxyterminal extension of Gag by T cell epitopes from human cytomegalovirus pp65 resulted in the formation of hybrid VLPs that strongly activated antigen-specific CD8 +  memory T cells  ex vivo . Besides being a carrier for polypeptides inducing antigen-specific immune responses  in vivo , VLP chimeras were also shown to be effective in the expression and purification of (i) a heterologous model protein (GFP), (ii) a  per se  toxic protein (K28 α-subunit), and (iii) a particle-associated and fully recyclable biotechnologically relevant enzyme (esterase A). Thus, yeast viral Gag represents a unique platform for the  in vivo  assembly of chimeric VLPs, equally attractive and useful in vaccine development and recombinant protein production.

Exploiting the Yeast L-A Viral Capsid for the In Vivo Assembly of Chimeric VLPs as Platform in Vaccine Development and Foreign Protein Expression