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Scorpion toxins that block potassium channels and antimicrobial plant defensins share a common structural CSαβ-motif. These toxins contain a toxin signature (K-C 4 -X-N) in their amino acid sequence, and based on  in silico  analysis of 18 plant defensin sequences, we noted the presence of a toxin signature (K-C 5 -R-G) in the amino acid sequence of the  Arabidopsis thaliana  defensin AtPDF2.3. We found that recombinant (r)AtPDF2.3 blocks K v 1.2 and K v 1.6 potassium channels, akin to the interaction between scorpion toxins and potassium channels. Moreover, rAtPDF2.3[G36N], a variant with a KCXN toxin signature (K-C 5 -R-N), is more potent in blocking K v 1.2 and K v 1.6 channels than rAtPDF2.3, whereas rAtPDF2.3[K33A], devoid of the toxin signature, is characterized by reduced K v  channel blocking activity. These findings highlight the importance of the KCXN scorpion toxin signature in the plant defensin sequence for blocking potassium channels. In addition, we found that rAtPDF2.3 inhibits the growth of  Saccharomyces cerevisiae  and that pathways regulating potassium transport and/or homeostasis confer tolerance of this yeast to rAtPDF2.3, indicating a role for potassium homeostasis in the fungal defence response towards rAtPDF2.3. Nevertheless, no differences in antifungal potency were observed between the rAtPDF2.3 variants, suggesting that antifungal activity and K v  channel inhibitory function are not linked.

The antifungal plant defensin AtPDF2.3 from Arabidopsis thaliana blocks potassium channels