Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens

Abstract

Four homogeneous proteins (Cw,,, Cw,,, Cw2,. Cw,,) were isolated from etiolated barley leaves by extraction of the insoluble pellet from a Tris-HCI (pH 7.5) homogenate with 1.5 M LiCl and fractionation by reverse-phase high-performance liquid chromatography. All 4 proteins inhibited growth of the pathogen Cfavibacter michiganensis subsp. sepedonicus (E&s = l-3 x IO-' M) and had closely related N-terminal amino acid sequences. The complete amino acid sequences of proteins Cw,, and Cw,, were determined and found to be homologous to previously described, non-specific lipid transfer proteins from plants (32-628 identical positions). The proteins also inhibited growth of the bacterial pathogen Pseudomonas solanacearum (E&s = 3-6 x IO-' M) and the fungus Fusarium solani (EC,,s = 3-20 x 10m6 M). A homologous protein from maize leaves (Cw,,) was purified in a similar manner and also found to have inhibitory properties. A synergistic effect against the fungus was observed when protein Cw,, was combined with thionins. A defense role for non-specific lipid transfer proteins from plants is proposed.Lipid transfer protein; Plant pathogen; Thionin

Homology modelling and molecular dynamics aided analysis of ligand complexes demonstrates functional properties of lipid‐transfer proteins encoded by the barley low‐temperature‐inducible gene family, blt4

“…Because of their extracellular location and gene expression in epidermal cells, it has been suggested that, in vivo, they may be involved in cutin and surface wax deposition rather than lipid transfer (Sterk et al, 1991;Pyee et al, 1994). Lipid-transfer proteins extracted from barley and maize leaves have also been shown to be the potent inhibitors of bacterial and fungal plant pathogens (Molina et al, 1993), suggesting a third possible in vivo function for these proteins.…”

Differential effects of five types of antipathogenic plant peptides on model membranes

“…Fax (34) (4) 464-8500 nisms of action are available for the more recently described plant peptide families, such as the so-called lipid transfer proteins (LTP), which are extracellular peptides involved in plant defense against pathogens [10][11][12], and the DL1 and DL2 families of antipathogenic peptides, which may be phylogenetically related to each other and share some common features with snake-venom desintegrins [ [13], M. Moreno et al, in preparation]. From the structural point of view, LTP2 from barley is known to contain 90 amino acid residues, with a positive charge/mass ratio of 0.9 X 10~3 [10], while no equivalent data are available for the DL1 and DL2 peptides. In summary, all the peptides tested are water-soluble and, as far as we know, all are positively charged at neutral pH and appear to have a compact globular conformation.…”

Cloning and Expression of Ragweed Allergen Amb a 6

“…Among these are proteins from tobacco (accession no. U14168), barley [34] and wheat [28]. Another homologous sequence which appears to be a member of this family is derived from a major allergen in Parietaria [29].…”

“…᭧ 1998 Blackwell Science Ltd, Scandinavian Journal of Immunology, 48, [26][27][28][29][30][31][32][33][34][35][36] days, a sample of supernatant was taken from each flask and 0.5% MeOH was added to each. rAmb a 6 production was monitored by SDS-PAGE and Western blot analysis.…”