Genes encoding hevein-like defense peptides in wheat: distribution, evolution, and role in stress response.

Hevein-like plant defense peptides WAMP-1a/b with a unique 10-Cys motif are found in the wheat Triticum kiharae seeds. Three different wamp genomic and cDNA sequences were derived from T. kiharae; no introns were spotted in the protein-coding regions of the genes. The deduced Wamp precursor proteins consist of a signal peptide, mature peptide (WAMP) and C-terminal prosequence. Origin of WAMPs from class I/IV chitinases via deletion of the catalytic domain is proposed based on homology between their genes. Genome screening of several cereals and goatgrasses from the genera Triticum and Aegilops was performed. No wamp homologues were identified in Triticum monococcum (A(b)A(b)) or Triticum urartu (A(u)A(u)), diploid species with an A genome. To the contrary, highly homologous wamp genes were discovered in hexaploid Triticum aestivum (A(u)A(u)BBDD) and T. kiharae (A(b)A(b)GGDD), and the putative genome donors Triticum timopheevii (A(b)A(b)GG), Aegilops speltoides (BB), and Aegilops tauschii (DD), providing strong evidence for the ancient origin of these genes and their association with the B, D and G genomes. The role of T. kiharae WAMPs in biotic stress is suggested by their antifungal activity and increased accumulation of wamp transcripts in response to phytopathogen challenge. Differential reaction to fungi was demonstrated: Fusarium oxysporum enhanced expression of wamp genes, whereas Aspergillus niger induced transcription reprogramming and alternative polyadenylation. WAMPs participate in plant response also to abiotic stress. Although no changes were noted at elevated or decreased temperatures, high salt concentrations enhanced wamp expression, the first indication of hevein-type peptide participation in salinity stress.