tailieunhanh - Báo cáo khoa học: 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 kiharaeDorof. et Migusch. | A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif Tatyana I. Odintsova1 Alexander A. Vassilevski2 Anna A. Slavokhotova1 Alexander K. Musolyamov2 Ekaterina I. Finkina2 Natalia V. Khadeeva1 Eugene A. Rogozhin2 Tatyana V. Korostyleva1 Vitalii A. Pukhalsky1 Eugene V. Grishin2 and Tsezi A. Egorov2 1 Vavilov Institute of GeneralGenetics Russian Academy of Sciences Moscow Russia 2 Shemyakin Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russia Keywords antifungal peptide chitin-binding cysteine motif recombinant peptide Triticum kiharae Correspondence T. Egorov Shemyakin Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences ul. Miklukho-Maklaya 16 10 117997 Moscow Russia Fax 7 495 330 7301 Tel 7 495 3364022 E-mail ego@ Database The protein sequences reported in this paper have been submitted to the UniProtKB database under the accession number P85966 Received 7 April2009 revised 1 June 2009 accepted 5 June 2009 doi 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 .