The optimized capsid gene of porcine circovirus type 2 expressed in yeast forms virus-like particles and elicits antibody responses in mice fed with recombinant yeast extracts

Secretory expression of Porcine Circovirus Type 2 capsid protein in Pichia pastoris

“…Glycosylation sites have been found for this protein (Hamel et al, 1998), and a variation in the protein mobility was observed when the production of the protein was compared in different recombinant systems (Bucarey et al, 2009), which may explain their different sizes. Nevertheless, the results presented here are in agreement with those of Tu et al (2012), which found the PCV2 cap protein in a similar molecular weight.…”

“…However it is recognized that this sequence represents an important domain for the formation of the inner surface of the virion (Lekcharoensuk et al, 2004;Wu et al, 2012). Alternatively, the expression of rCap protein in eukaryotic systems, such as yeast (S. cerevisiae), insect cells and mammalian cells has been used successfully (Fan et al, 2007;Bucarey et al, 2009;Júnior et al, 2009). However, yeast cultures are easy to maintain, which makes them faster and less expensive to use than other eukaryotic expression systems.…”

“…Bucarey et al (2009) reported that to produce the PCV2 Cap protein in S. cerevisiae was necessary to optimize the gene, suggesting that the codon usage derived from the wild Cap gene negatively affects the metabolism of the yeast. In view of this, in this study, the Cap gene was codon-optimized for expression in P. pastoris, and the codon usage frequency between the Cap gene and the yeast P. pastoris was reduced from 19% to 10% after the codon optimization.…”

Recombinant Flagellin-Porcine Circovirus Type 2 Cap Fusion Protein Promotes Protective Immune Responses in Mice

“…Although mice may not be an ideal animal model to resemble PCV2 infection as observed for pigs [36], PCV2 can infect and replicate in some mouse strains including BALB/c mouse when used with the appropriate inoculating dose and administered route [35,37]. Therefore, the mouse model has been used for evaluating the immunogenicity and protection of PCV2 vaccines [11,14,38–40]. In the present study, we used the BALB/c mouse model for evaluating the immunogenicity and protective capabilities of an experimental vaccine based on the recombinant flagellin-Cap fusion protein expressed in the baculovirus system.…”

Generation of recombinant porcine parvovirus virus-like particles in Saccharomyces cerevisiae and development of virus-specific monoclonal antibodies

“…To our knowledge, our study provides the first evidence of stable recombinant PPV VP2 VLPs not produced in baculovirus expression system. S. cerevisiae expression system has been shown to be efficient in producing antigenic VLPs of diagnostic relevance of human parvoviruses [28,29] and porcine circovirus [39]. Therefore, it represents a potential system to meet the need for VLP-forming antigens to detect and differentiate a number of newly discovered porcine.…”