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A novel antifungal hevein‐type peptide from Triticum kiharae seeds with a unique 10‐cysteine motif
Author(s) -
Odintsova Tatyana I.,
Vassilevski Alexander A.,
Slavokhotova Anna A.,
Musolyamov Alexander K.,
Finkina Ekaterina I.,
Khadeeva Natalia V.,
Rogozhin Eugene A.,
Korostyleva Tatyana V.,
Pukhalsky Vitalii A.,
Grishin Eugene V.,
Egorov Tsezi A.
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07135.x
Subject(s) - cysteine , peptide , chitin , serine , biochemistry , recombinant dna , residue (chemistry) , biology , amino acid , cyclic peptide , escherichia coli , glycine , gene , enzyme , chitosan
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 IC 50 values 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.