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Fig. 3 | Parasites & Vectors

Fig. 3

From: Bacillus subtilis spore with surface display of paramyosin from Clonorchis sinensis potentializes a promising oral vaccine candidate

Fig. 3

Expression identification and thermostability analysis of CotC-CsPmy on B. subtilis spores. a SDS-PAGE analysis of the fusion expression on B. subtilis spores in different sporulation times. The arrows indicated the possible expression band. The molecular mass of fusion protein was approximately 108.8 kDa. b Identification of CotC-CsPmy fusion protein with Western blotting by using rat anti-rCsPmy serum. There was no corresponding band in lanes of B.s-CotC spores and the supernatant of B.s-CotC-CsPmy spores. c Thermostability analysis of fusion protein on B. subtilis spores. An equal quantity of spore was packaged in Eppendorf tubes and stored at RT, 4 °C, -40 °C, or -80 °C for 3 months, and then analyzed by using 12% SDS-PAGE. Lane M: Molecular weight marker; Lane 1: B.s-CotC spores stored at -80 °C; Lanes 2–5: B.s-CotC-CsPmy stored at room temperature, 4 °C, -40 °C or -80 °C, respectively. The fusion protein bands are indicated by arrows

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