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Continuous-Elution Electrophoresis for Purification of the Baculovirus-Expressed Coronavirus Structural Proteins, Rev A

a minor, virus-specific band of 100 kDa was detected on both polyacrylamide gels and nitrocellulose membranes (Figure 3B, C, lane 5). The resulting purified S-protein concentration was 0.15 mg/ml or 2% of the initial baculovirus lysate.


Discussion

The production of subunit viral vaccines requires the purification of the immunogens of interest from other cellular proteins. The CE-PAGE represents an approach whereby proteins are electrophoretically separated based on their molecular size and collected in fractions.

The yields of purified M-, N- and S-proteins corresponding to the 18 x 105 Sf9 insect cells (0.5, 0.4 and 0.15 mg/ml, respectively) are reflective of the levels of recombinant protein expected (28%) and in agreement with data published on the efficiency of the baculovirus expression system (Luckow et al., 1988). Elution of small volumes of purified, concentrated proteins (0.20.5 ml) reflects the capacity of the Mini Prep Cell system, but can be scaled up when larger amounts are required by using the same conditions and a Model 491 Prep Cell.

By western blotting of the purified proteins with porcine hyperimmune antiserum to TGEV (S, M, N) in western blot and the ELISA reaction with monoclonal antibodies (S, N), we demonstrated that immunogenic and neutralizing epitopes were preserved on the purified proteins. On both polyacrylamide gels and nitrocellulose membranes, a minor 100 kDa protein band in addition to the major 150 kDa protein was detected for the TGEV-S protein (Figure 3B, C, lane 5). This most likely reflected the presence of an immature, posttranslationally non-modified form of S-glycoprotein as previously reporte
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