FIG 1.

VdHP1 was a hydrophobic protein and induced hypersensitive response. (A) The VdHP1 amino acid sequence aligned between VdHP1, cerato-ulmin from O. ulmi (80), T. reesei HFB1 (81), cryopyrin from C. parasitica (82), and VDH1 from V. dahliae (8, 31). Identical residues were shaded black, similar residues were shaded blue or pink, and cysteine residues were marked with asterisks or red dotted box. The signal peptide of VdHP1 was marked by a solid red box. (B) Conformation of the function of the signal peptide of VdHP1 by yeast secretion trap assay. (C) VdHP1 induced hypersensitive response on N. benthamiana leaves. The numbers 1, 2, 3, and 4 represent a one-to-one correspondence in gels. Semi-quantitative RT-PCR (sqRT-PCR) analysis of transiently expressed VdHP1 in N. benthamiana leaves. NbActin was used as the control. The gels are agarose gels (0.1%). Scale bar = 0.5 cm.