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Fig. 4 | BMC Biology

Fig. 4

From: Verticillium dahliae CFEM proteins manipulate host immunity and differentially contribute to virulence

Fig. 4

Cysteine residues in the CFEM domains of VdSCP76 and VdSCP77 are essential for immunity suppression. A The primary structures and putative disulfide bonds (DBs) of VdSCP76 and VdSCP77. Pink, blue, and orange blocks indicated as signal peptide, CFEM domain, and unidentified sequence. Vertical strings represented cysteine residues sites position. B, C The cell death suppression activity of the wild-type, truncated proteins, and cysteine residue site-directed mutant proteins of VdSCP76 and VdSCP77 were determined by transient co-expression with VdEG1, respectively, in 4-week-old Nicotiana benthamiana leaves. “CA” indicates that all cysteine residues were replaced with alanine. GFP and VdEG1 were used as controls. D, E The function of single cysteine residues in VdSCP76 and VdSCP77 were detected by cell death inhibition against VdEG1 assays in 4-week-old N. benthamiana leaves. “C-No.-A” represents the single cysteine residue replaced with alanine in the respective position in VdSCP76 and VdSCP77. The efficiency of transient expression of the cell death-inducing gene VdEG1 was validated by western blotting with FLAG tag antibody and horseradish peroxidase (HRP)-linked immunoassay. Ponceau S-stained Rubisco protein is shown as a total protein loading control

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