Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of <i>Arabidopsis</i> and spinach

Segura, Ana; Moreno, M. L.; Garcı́a-Olmedo, Francisco

doi:10.1016/0014-5793(93)80641-7

Cited by 125 publications

(71 citation statements)

References 15 publications

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“…There are many reports confirming their extracellular or cell wall localization (Bernhard et al, 1991;Sterk et al, 1991;Segura et al, 1993;Thoma et al, 1993Thoma et al, , 1994. The 140-to 204-amino acid LTPLs identified in this screen are somewhat larger than LTPs, which are less than 120 amino acids.…”

Section: Ltpl Proteins (18)mentioning

confidence: 97%

Prediction of Glycosylphosphatidylinositol-Anchored Proteins in Arabidopsis. A Genomic Analysis

et al. 2002

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Glycosylphosphatidylinositol (GPI) anchoring of proteins provides a potential mechanism for targeting to the plant plasma membrane and cell wall. However, relatively few such proteins have been identified. Here, we develop a procedure for database analysis to identify GPI-anchored proteins (GAP) based on their possession of common features. In a comprehensive search of the annotated Arabidopsis genome, we identified 167 novel putative GAP in addition to the 43 previously described candidates. Many of these 210 proteins show similarity to characterized cell surface proteins. The predicted GAP include homologs of ␤-1,3-glucanases (16), metallo-and aspartyl proteases (13), glycerophosphodiesterases (6), phytocyanins (25), multi-copper oxidases (2), extensins (6), plasma membrane receptors (19), and lipid-transfer-proteins (18). Classical arabinogalactan (AG) proteins (13), AG peptides (9), fasciclin-like proteins (20), COBRA and 10 homologs, and novel potential signaling peptides that we name GAPEPs (8) were also identified. A further 34 proteins of unknown function were predicted to be GPI anchored. A surprising finding was that over 40% of the proteins identified here have probable AG glycosylation modules, suggesting that AG glycosylation of cell surface proteins is widespread. This analysis shows that GPI anchoring is likely to be a major modification in plants that is used to target a specific subset of proteins to the cell surface for extracellular matrix remodeling and signaling.Conventional membrane proteins possess one or more transmembrane domains that traverse the hydrophobic lipid bilayer. A glycosylphosphatidylinositol (GPI) anchor is an alternative means of attaching a protein to the membrane (for review, see Udenfriend and Kodukula, 1995), and it is found in all eukaryotic organisms. The C terminus of a GPIanchored protein (GAP) is covalently attached via phosphoethanolamine and a conserved glycan to phosphatidylinositol or a ceramide (Kinoshita and Inoue, 2000). GAPs have many features that distinguish them from proteins with transmembrane domains. The anchor can be removed by the action of specific phospholipases (Griffith and Ryan, 1999), converting the protein into a water-soluble form. In many organisms, they are found specifically at the outer leaflet of the plasma membrane (PM). It is important that GPI anchoring can target proteins to the PM in a polarized or localized manner, for example to the apical membrane of polarized mammalian epithelial cells (Le Gall et al., 1995) or the axon of neurons (Brown et al., 2000). As part of this targeting mechanism, GAPs are thought to associate with lipid rafts (Muniz and Riezman, 2000;Ikonen, 2001), and there is evidence for rafting of GAPs in plants ( Peskan et al., 2000). Therefore, this class of proteins forms a potentially important group of molecules involved in plant cell surface generation and remodeling (Sherrier et al., 1999).GAPs have only relatively recently been discovered in plants. Arabinogalactan (AG) proteins (AGPs), cell surface proteo...

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Section: Ltpl Proteins (18)mentioning

confidence: 97%

Prediction of Glycosylphosphatidylinositol-Anchored Proteins in Arabidopsis. A Genomic Analysis

et al. 2002

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“…W-FABP was not active against the test microorganism at up to l0/2M concentration, tenfold higher than those giving complete inhibition with LTPs or with thionins [10,13], which were used as positive controls in the experiment (not shown).…”

Section: A Castagnaro E Garcia-olmedol Febs Letters 349 (1994) 117-mentioning

confidence: 99%

A fatty‐acid‐binding protein from wheat kernels

Castagnaro¹,

Garcı́a-Olmedo²

1994

FEBS Letters

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A protein of about 7 kDa (W-FABP) has been isolated from mature wheat kernels by H,O extraction and gel filtration of the extract, followed by two steps of high-performance liquid chromatography. The N-terminal amino acid sequence has been determined up to the 28th residue and found to be identical (except for positions 4 and 5) to that deduced from a barley cDNA (EMBL X15257), which had been improperly classified as a non-specific lipid transfer protein (LTP2). Similarly with LTPs, W-FABP does bind fatty acids, but in contrast, it is not significantly homologous to LTPs, it is not recognized by LTP antibodies, it has a more acidic isoelectric point (pH < 6.8 vs. pH > 9.6), and it does not show antibiotic properties.

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“…Little information concerning possible mecha-*Corresponding author. 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.…”

Section: Introductionmentioning

confidence: 99%

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

Caaveiro

Molina²,

González-Mañas

et al. 1997

FEBS Letters

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The effects of five antipathogenic plant peptides, wheat a-thionin, potato PTH1 defensin, barley LTP2 lipid transfer protein, and potato tuber DL1 and DL2 defensins, have been tested against phospholipid vesicles (liposomes). Wheat thionin very actively induces aggregation and leakage of negatively charged vesicles. LTP2 displays the same activities, although to a limited extent. Under certain conditions PTH1 and DL2 induce vesicle aggregation, but not leakage. Potato defensin DL1 failed to show any effect on liposomes. The same peptides have been assayed against a plant pathogenic bacterium, both the membrane-active and -inactive compounds having efficient antibacterial action.

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Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach

Cited by 125 publications

References 15 publications

Prediction of Glycosylphosphatidylinositol-Anchored Proteins in Arabidopsis. A Genomic Analysis

Prediction of Glycosylphosphatidylinositol-Anchored Proteins in Arabidopsis. A Genomic Analysis

A fatty‐acid‐binding protein from wheat kernels

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

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