Extended Data Fig. 1: The FgLPMO9A encodes an apoplastic effector protein.
a, FgLPMO9A and FgLPMO9AH107A do not induce cell death in N. benthamiana. b, Alignment of the homologous amino acid sequence of FgLPMO9A in the Fusarium genus. Sequence similarity is represented in blue, and red asterisks indicate copper ion binding sites. c, AlphaFold3-predicted protein structure of FgLPMO9A, highlighting the copper ion binding sites. d, Signal peptide prediction of FgLPMO9A using SignalP 6.0. e, Functional validation of the FgLPMO9A signal peptide in the yeast Saccharomyces cerevisiae YTK12 strain. Yeast carrying the FgLPMO9A signal peptide fused to the pSUC2 vector was able to grow on CMD-W and YPRAA media. pSUC2-Avr1bSP served as the positive control, while pSUC2-Mg87SP served as the negative control. Secreted invertase catalyzes the reduction of 2,3,5-triphenyltetrazolium chloride (TTC) to form insoluble red 1,3,5-triphenyl formazan (TPF). f, Subcellular localization of FgLPMO9A and FgLPMO9AΔSP in N. benthamiana before and after plasmolysis. FgLPMO9A-mCherry and FgLPMO9AΔSP-mCherry were transiently expressed, with GFP and mCherry empty vectors used as controls. After plasmolysis, the white dashed lines indicate the cell wall structure. Bar = 20 μm. These experiments were repeated 3 times with similar results.
