Fusarium head blight is a devastating disease of wheat. Fhb1 is the most widely used quantitative trait locus in wheat cultivars globally providing type-2 resistance against Fusarium graminearum. Previously, using mutation analysis, gene silencing, and overexpression, a Pore-forming toxin-like (PFT) protein was shown to underlie the Fhb1-mediated resistance in wheat by Rawat et al (2016). PFT is a chimeric plant lectin with two agglutinin domains of Amaranthus caudatus and one bacterial toxin domain of the aerolysin pore-forming toxin family of bacterial toxins. In the present work, heterologous expression of wheat-PFT was done in Arabidopsis ecotype Landsberg erecta. The transgenic Arabidopsis plants were challenged with multiple fungal pathogens including F. graminearum, Colletotrichum higginsianum, Sclerotinia sclerotiorum, and Botrytis cinerea. The wheat PFT was found to provide a broad spectrum resistance against all the tested fungal pathogens in the T₂ and T₃ generation of the transgenic Arabidopsis plants. However, the transgenic plants were not resistant to bacterial and oomycete pathogens Pseudomonas syringae and Phytophthora capsici, respectively. To investigate the underlying cause of the specific resistance of wheat PFT to fungal pathogens and not bacterial and oomycete pathogens, PFT protein was expressed in Nicotiana followed by its extraction and purification. The purified PFT protein wash was hybridized to an array of 300 different carbohydrate monomers and oligomers. Interestingly, glycan microarray assay revealed that PFT specifically binds to chitin monomer, N-Acetyl glucosamine (GlcNAc), which is an exclusive component of fungal cell walls and is not present in bacteria or Oomycete. Together, these results that suggest PFT is an atypical broad-spectrum disease-resistance protein that may contribute to resistance against a wide range of fungal pathogens in multiple crop plants.