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

blue), heated at 95 C for 4 min and stored at 20 C until used for preparative electrophoresis.

A Mini Prep Cell (Bio-Rad Laboratories, Hercules, CA) system was used to perform continuous-elution polyacrylamide gel electrophoresis (CE-PAGE) with conditions modified for each TGEV protein to be purified. For the TGEV M-protein, the sample (0.5 ml, corresponding to 18 x 105 cells) was layered onto a 4% (1.5 cm) polyacrylamide stacking gel with a 10% (8 cm) polyacrylamide separating gel. Proteins were electrophoresed under denaturing conditions at constant voltage (200 V) for 3.5 h with a flow rate of 0.05 ml/min. After 3.5 h, fractions were collected in 5 min intervals (0.25 ml/fraction) with a total of 30 fractions. For the TGEV N-protein electrophoresis was performed as described above, but for 4.5 h prior to collection of 30 fractions. For the TGEV S-protein; the sample (0.5 ml, corresponding to 18 x 105 cells) was layered onto a 4% (1.5 cm) polyacrylamide stacking gel with a 6% (8 cm) polyacrylamide separating gel in the Mini Prep Cell gel tube assembly. Electrophoresis was performed as described above for 8.5 h prior to collection of the 30 fractions.

Selected protein fractions were examined by electrophoresis in analytical polyacrylamide slab gels and stained with Coomassie blue (Wu and Welsh, 1996). The fractions of desired molecular weight were pooled and concentrated using Centricon devices (Amicon, Beverly, MA) with a 10 kDa cutoff for the M-protein, and a 30 kDa cutoff for the N- and S-proteins. Virus specificity of the M-, N-, and S-proteins and conformational stability of the N-protein and epitopes A and D of the S-protein were confirmed by immunoblo
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