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 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.
Odintsova
Tatyana I
TI
Vavilov Institute of General Genetics, Russian Academy of Sciences, Moscow, Russia.
Vassilevski
Alexander A
AA
Slavokhotova
Anna A
AA
Musolyamov
Alexander K
AK
Finkina
Ekaterina I
EI
Khadeeva
Natalia V
NV
Rogozhin
Eugene A
EA
Korostyleva
Tatyana V
TV
Pukhalsky
Vitalii A
VA
Grishin
Eugene V
EV
Egorov
Tsezi A
TA
D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000302:isolation & purification*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D001665:Binding Sites; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D011994:Recombinant Proteins / Q000737:chemistry; D012639:Seeds / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014908:Triticum / Q000737:chemistry*
D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D037121:Plant Lectins; D011994:Recombinant Proteins; C045875:hevein