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Guerbette, F.; Grosbois, Michèle; Jolliot-Croquin, Alain; Kader, Jean‐Claude; Zachowski, Alain

doi:10.1023/a:1006870220172

Cited by 27 publications

(9 citation statements)

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“…Ns-LTP2 of all tested LTPs from N. sativa seeds had a more pronounced ability than LTP1 and LTP3 to induce release of ANTS from the PC liposome inner volume and especially from negatively charged liposomes formed from 90% PC + 10% DMPS. This agreed with the literature [13]. This also confirmed the conclusion that the presence of anionic lipids in model and biological membranes increases the probability of forming pores or defects through which small organic molecules and inorganic ions can flow.…”

supporting

confidence: 92%

Interaction of lipid-transport proteins from Nigella sativa seeds with lipid membranes

et al. 2010

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Three pure lipid-transport proteins (LTPs) were isolated from Nigella sativa seeds. The effects of the three LTPs on release of ANTS probe from the inner volume were studied using fluorescence in liposomes of different lipid composition. It was shown that all LTPs had a dose-dependent effect on the liposome permeability.Non-specific lipid-transport proteins (LTPs) belong to a family of proteins that are widely distributed in plants [1,2]. They were isolated from seeds of various classes of plants such as maize [3], wheat [4], barley [5], and rice [6] in addition to leaves of several plants [7]. A comparison of the physicochemical properties of the isolated compounds reveals common trends in the molecular structure. They are a homogeneous family of basic peptides 90-93 amino acids long with eight cysteine units in conserved positions that form a hydrophobic cavity [8]. LTPs are typically capable in vitro of transferring glycerophospholipids or galactolipids through membranes [1, 8]. They can inhibit in vivo the growth of bacteria and fungi [8]. One of the proposed mechanisms of the antifungal activity of several LTPs (Ha-AP10 from Helianthus annuus [9], LTP2 from wheat [10], and LTP from onion [11]) is the induction by them of increased permeability of pathogen plasmatic membranes for small organic molecules and inorganic ions.It would be useful to find trends in their effects on the structural properties of lipid membranes in order to understand better differences in the effectiveness with which LTP from various sources interact with lipids.Our goal was to study the effects of three LTP isolated from Nigella sativa seeds (Ns-LTPs) that had different physicochemical properties (LTP1, LTP2, LTP3) on the permeability of model lipid membranes.We have previously isolated and studied the physicochemical properties of Ns-LTP1 from N. sativa seeds [12]. Here we continued the detailed investigation of the peptide composition from N. sativa seeds and found two more peptides that belonged to the same class as LTP1 but had different molecular weights (MWs).Chromatography of total peptides from N. sativa seeds over affinity sorbent Hi Trap Heparin HP produced four basic fractions that were eluted by different NaCl concentrations (0 M, 0.1, 0.5, and 1). According to mass spectrometry, a component with MW 8130 Da dominated the fraction eluted by buffer A. Then, the component was purified by RP-HPLC, which produced four fractions. Mass spectral analysis of these showed that fraction 4 was homogeneous and contained a polypeptide of MW 8130 Da (LTP2).The 0.1-M fraction contained several protein components with MW in the range 9-12 kDa. The dominant polypeptide had MW 9602 Da. The polypeptide was purified by RP-HPLC, which produced eight fractions. Mass spectral analysis of these showed that fraction 4 was homogeneous and contained a component with MW 9602 Da, which we called Ns-LTP1. We sequenced its N-terminus and determined the amino-acid composition and number of cysteines in order to confirm that it was an LTP [12].

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confidence: 92%

Interaction of lipid-transport proteins from Nigella sativa seeds with lipid membranes

et al. 2010

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“…Because cellular membranes are thought to be the primary sites of damage due to cold stress, changes in the membrane behaviour under cold conditions must be critical to the development of freezing tolerance. Several plant LTPs are known to interact with lipids and fatty acids in vitro without ligand specificity (Zachowski et al, 1998; Guerbette et al, 1999; Hamilton, 2004). They may function as lipid carriers between intracellular organelles (Kader et al, 1984), and play a role in the delivery of wax components during the assembly of the cuticle (Sterk et al, 1991; Yeats and Rose, 2008; Debono et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Lipid transfer protein 3 as a target of MYB96 mediates freezing and drought stress in Arabidopsis

Guo

Yang

Zhang

et al. 2013

Journal of Experimental Botany

240

175

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Several lipid-transfer proteins were reported to modulate the plant response to biotic stress; however, whether lipid-transfer proteins are also involved in abiotic stress remains unknown. This study characterized the function of a lipid-transfer protein, LTP3, during freezing and drought stress. LTP3 was expressed ubiquitously and the LTP3 protein was localized to the cytoplasm. A biochemical study showed that LTP3 was able to bind to lipids. Overexpression of LTP3 resulted in constitutively enhanced freezing tolerance without affecting the expression of CBFs and their target COR genes. Further analyses showed that LTP3 was positively regulated by MYB96 via the direct binding to the LTP3 promoter; consistently, transgenic plants overexpressing MYB96 exhibited enhanced freezing tolerance. This study also found that the loss-of-function mutant ltp3 was sensitive to drought stress, whereas overexpressing plants were drought tolerant, phenotypes reminiscent of myb96 mutant plants and MYB96-overexpressing plants. Taken together, these results demonstrate that LTP3 acts as a target of MYB96 to be involved in plant tolerance to freezing and drought stress.

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“…LTPs are a class of conserved plant proteins widely distributed in nature [26]. They belong to a family of polypeptides (90–95 amino acids) involved in plant defense mechanisms against pathogens and environmental stress [27].…”

Section: Discussionmentioning

confidence: 99%

Wine Anaphylaxis in a German Patient: IgE-Mediated Allergy against a Lipid Transfer Protein of Grapes

Schäd

Trcka

Vieths

et al. 2005

Int Arch Allergy Immunol

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Background: IgE-mediated allergy to grapes has very rarely been reported in patients from the Mediterranean area. Recently, endochitinase 4 and a lipid transfer protein (LTP) have been identified as major allergens in grape-allergic patients who do not have an associated pollinosis. The purpose of this case study was to identify the allergens responsible for severe anaphylactic reactions after consumption of wine, fresh grapes and raisins in a German patient. Methods: Prick-to-prick tests and the basophil activation test (BAT) were performed to confirm allergy. Specific IgE was further analyzed by immunoblotting and inhibition tests for the determination of crossreactivity. The IgE-binding protein was subjected to N-terminal microsequencing. Results: Prick-to-prick tests were positive to fresh and cooked white and blue grapes, to raisins, to white and red wine, and to grape extract. Specific IgE against grapes (f259) was 2.43 kU/l (class 2). The BAT showed specific IgE-mediated activation of basophils after stimulation with grape extract. IgE binding to a 15-kDa protein was completely inhibited by pre-incubation with recombinant cherry LTP Pru av 3. N-terminal sequencing identified this 15-kDa protein as grape LTP Vit v 1. Conclusion: Our data show that sensitization to LTP can occur outside the Mediterranean area causing severe fruit allergy without association to pollinosis.

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Cited by 27 publications

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Interaction of lipid-transport proteins from Nigella sativa seeds with lipid membranes

Interaction of lipid-transport proteins from Nigella sativa seeds with lipid membranes

Lipid transfer protein 3 as a target of MYB96 mediates freezing and drought stress in Arabidopsis

Wine Anaphylaxis in a German Patient: IgE-Mediated Allergy against a Lipid Transfer Protein of Grapes

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