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Fig. 3 | BMC Biotechnology

Fig. 3

From: Optimized production of a biologically active Clostridium perfringens glycosyl hydrolase phage endolysin PlyCP41 in plants using virus-based systemic expression

Fig. 3

Plate lysis assay of protein samples on Clostridium perfringens Cp39 confluent plates. Spot assays were conducted as described in the Materials and Methods and a photographic image of the plate was taken 30 min after application of the samples. The contents of the wells are as follows: A1-A6, Negative control, His-purified fractions from E. coli: BL21 pET21a; B1- B4- plant virus samples in PBS buffer; B1 & B2-empty PVX virus; B3 & B4-PVX virus with PlyCP41p; B5-PBS buffer; B6-elution buffer control; C1-C4- plant virus samples in “10:90” buffer (50 mM NaH2PO4 pH 7.0, 30 mM NaCl, 25 mM imidazole, 3% glycerol). C1&C2-empty PVX; C3&C4-PVX with PlyCP41p; C5–10 μL PVX with PlyCP41p in PBS buffer; C6–10 μL PVX with PlyCP41p in PBS buffer; D1-D4- empty; D5–10 μL PVX with PlyCP41p in “10:90 buffer”; D6–10 μL PVX with PlyCP41p in “10:90 buffer” E1-E6- E. coli PlyCP41 fractions purified on Ni-NTA column (FT, W1, W2, E1, E2, E3); F1- F4–10 μg, 1 μg, 0.1 μg, 0.001 μg of PlyCP41; F5 10:90 buffer. Asterisks indicate the plant extracts containing the PlyCP41p protein

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