4.4 Article

Diversity of wheat anti-microbial peptides

Journal

PEPTIDES
Volume 26, Issue 11, Pages 2064-2073

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2005.03.007

Keywords

Triticum kiharae Dorof. et Migusch.; wheat; anti-microbial peptides; glycine-rich peptides; Defensins; thionins; lipid-transfer proteins; hevein-like peptides; knottin-like peptides; MBP-1 homologs

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From seeds of Triticum kiharae Dorof. et Migusch., 24 novel anti-microbial peptides were isolated and characterized by a combination of three-step HPLC (affinity, size-exclusion and reversed-phase) with matrix-assisted laser-desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry and Edman degradation. Based on sequence similarity and cysteine motifs, partially sequenced peptides were assigned to 7 families: defensins, thionins, lipid-transfer proteins, hevein-like peptides, knottin-like peptides, glycine-rich peptides, and MBP-1 homologs. A novel subfamily of defensins consisting of 6 peptides and a new family of glycine-rich (8 peptides with different repeat motifs) were identified. Three 6-cysteine knottin-like peptides represented by N- and C-terminally truncated variants revealed no sequence homology to any known plant anti-microbial peptides. A new 8-cysteine hevein-like peptide and three 4-cysteine peptides homologous to MBP-1 from maize were isolated. This is the first communication on the occurrence of nearly all families of plant anti-microbial peptides in a single species. (c) 2005 Elsevier Inc. All rights reserved.

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