FEBS J, 2009, 276(15):4266-4275

A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif

Two forms of a novel antimicrobial peptide (AMP), named WAMP-1a and WAMP-1b, that differ by a single C-terminal amino acid residue and belong to a new structural type of plant AMP were purified from seeds of Triticum kiharae Dorof. et Migusch. Although WAMP-1a and WAMP-1b share similarity with hevein-type peptides, they possess 10 cysteine residues arranged in a unique cysteine motif which is distinct from those described previously for plant AMPs, but is characteristic of the chitin-binding domains of cereal class I chitinases. An unusual substitution of a serine for a glycine residue in the chitin-binding domain was detected for the first time in hevein-like polypeptides. Recombinant WAMP-1a was successfully produced in Escherichia coli. This is the first case of high-yield production of a cysteine-rich plant AMP from a synthetic gene. Assays of recombinant WAMP-1a activity showed that the peptide possessed high broad-spectrum inhibitory activity against diverse chitin-containing and chitin-free pathogens, with IC50values in the micromolar range. The discovery of a new type of AMP active against structurally dissimilar microorganisms implies divergent modes of action and discloses the complexity of plant-microbe interactions. © 2009 FEBS.

Odintsova TI, Vassilevski AA, Slavokhotova AA, Musolyamov AK, Finkina EI, Khadeeva NV, Rogozhin EA, Korostyleva TV, Pukhalsky VA, Grishin EV, Egorov TA

IBCH: 5504
Ссылка на статью в журнале: http://doi.wiley.com/10.1111/j.1742-4658.2009.07135.x
Кол-во цитирований на 03.2024: 73
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