Novel defensin subfamily from spinach (Spinacia oleracea)
Open Access
- 18 September 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 435 (2-3) , 159-162
- https://doi.org/10.1016/s0014-5793(98)01060-6
Abstract
Antimicrobial peptides (So-D1-7) were isolated from a crude cell wall preparation from spinach leaves (Spinacia oleracea cv. Matador) and, judged from their amino acid sequences, six of them (So-D2-7) represented a novel structural subfamily of plant defensins (group IV). Group-IV defensins were also functionally distinct from those of groups I–III. They were active at concentrations Clavibacter michiganensis) and Gram-negative (Ralstonia solanacearum) bacterial pathogens, as well as against fungi, such as Fusarium culmorum, F. solani, Bipolaris maydis, and Colletotrichum lagenarium. Fungal inhibition occurred without hyphal branching. Group-IV defensins were preferentially distributed in the epidermal cell layer of leaves and in the subepidermal region of stems.Keywords
This publication has 22 references indexed in Scilit:
- Antimicrobial Peptides from PlantsCritical Reviews in Plant Sciences, 1997
- Fungal Membrane Responses Induced by Plant Defensins and ThioninsJournal of Biological Chemistry, 1996
- Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and SaxifragaceaeFEBS Letters, 1995
- Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinachFEBS Letters, 1993
- Novel antimicrobial peptides from skin secretion of the European frog Rana esculentaFEBS Letters, 1993
- Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogensFEBS Letters, 1993
- Solution structure of .gamma.1-H and .gamma.1-P thionins from barley and wheat endosperm determined by proton NMR: a structural motif common to toxic arthropod proteinsBiochemistry, 1993
- Two-dimensional1H NMR study of recombinant insect defensin A in water: Resonance assignments, secondary structure and global foldingJournal of Biomolecular NMR, 1992
- A new family of small (5 kDa) protein inhibitors of insect α‐amylases from seeds or sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat γ‐purothioninsFEBS Letters, 1991
- An automated quantitative assay for fungal growth inhibitionFEMS Microbiology Letters, 1990