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. 2021 Jan 8;9(1):33. doi: 10.3390/vaccines9010033

Figure 1.

Figure 1

Purification of papaya mosaic virus with peptide at the N-terminus (PapMV-N) coat protein (CP). (A) Schematic representation of the intein–PapMV-N CP construct cloned in the pTWIN1 vector and expressed in Escherichia coli. The N-terminal methionine of the fusion protein is shown with a M. The site of cleavage by the intein is illustrated with scissors. Upon cleavage, the N-terminus of the PapMV-N CP presents GGGG at its N-terminus. The PapMV-N CP harbors a 6His-tag at its C-terminus to ease the purification process. (B) SDS-PAGE revealing the protein content of samples taken at successive purification steps of the PapMV-N CP. Molecular weight markers are shown to the left. Signals corresponding to the fusion protein (49.3 kDa), the cleaved intein (25.2 kDa), and the cleaved PapMV-N CP (24.1 kDa) are indicated on the right. Lanes: 1 lysate of induced bacteria producing the recombinant fusion protein; 2 fusion protein purified on ion matrix affinity chromatography (IMAC); 3 cleavage products; 4 purified PapMV-N CP.