Phylogenetic characterization and antifungal activity of recombinant defensin protein from Triticum aestivum


Defensins protein plays an important role in innate immune defense against infectious diseases in animals and plants. In our study and for the first time, common wheat (Triticum aestivum) defensin gene was fully characterized. The protein encodes from a signal peptide region of 25 amino acids. Homology searches showed that T. aestivum defensin have a highest identity (72-64 %) with other defensin selected sequences. A multiple sequence alignment indicates very well highly conserved regions include eight cystiene residues, α-helix, loop, and β-sheet. A phylogenetic analysis of the T. aestivum defensin gene sequence among other plant defensin sequences further confirmed that the T. aestivum sequence is very closely related to Triticum durum defensin sequences, and thus, is likely to have the same expressed structure and function. Moreover, the recombinant defensin protein was expressed in vitro and it show a strong antifungal activity against pathogenic strain Puccinia striiformis. Our study indicate that recombinant defensin protein may be a powerful tool for common wheat treatment.