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Thaumatin-like Protein (thaumatin-like + protein)
Selected AbstractsProteomic analysis of bacterial-blight defense-responsive proteins in rice leaf bladesPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 22 2006Tariq Mahmood Abstract Plants exhibit resistance against incompatible pathogens, via localized and systemic responses as part of an integrated defense mechanism. To study the compatible and incompatible interactions between rice and bacteria, a proteomic approach was applied. Rice cv. Java 14 seedlings were inoculated with compatible (Xo7435) and incompatible (T7174) races of Xanthomonasoryzae pv. oryzae (Xoo). Cytosolic and membrane proteins were fractionated from the leaf blades and separated by 2-D PAGE. From 366 proteins analyzed, 20 were differentially expressed in response to bacterial inoculation. These proteins were categorized into classes related to energy (30%), metabolism (20%), and defense (20%). Among the 20 proteins, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit (RuBisCO LSU) was fragmented into two smaller proteins by T7174 and Xo7435 inoculation. Treatment with jasmonic acid (JA), a signaling molecule in plant defense responses, changed the level of protein accumulation for 5 of the 20 proteins. Thaumatin-like protein and probenazole-inducible protein (PBZ) were commonly up-regulated by T7174 and Xo7435 inoculation and JA treatment. These results suggest that synthesis of the defense-related thaumatin-like protein and PBZ are stimulated by JA in the defense response pathway of rice against bacterial blight. [source] Thaumatin-like proteins , a new family of pollen and fruit allergensALLERGY, Issue 5 2004Heimo Breiteneder No abstract is available for this article. [source] Characterization of peach thaumatin-like proteins and their identification as major peach allergensCLINICAL & EXPERIMENTAL ALLERGY, Issue 9 2010A. Palacín Summary Background Peach is the most important fruit related to food allergy in the Mediterranean area. Pru p 3, its lipid transfer protein, has been described as the principal allergen responsible for cross-reactivities with other foods and pollen and the severity of clinical symptoms. However, the involvement of other allergenic families cannot be ruled out. Thaumatin-like proteins (TLPs) have been described as food allergen in several fruits, such as apple, cherry, kiwi and banana, and pollen. Objective To identify members of the TLP family in peach fruit and to characterize putative allergens. Methods Through two-dimensional (2D) electrophoresis of peach extract and immunodetections with a pool of peach-allergic patients, IgE-binding spots were identified and the corresponding proteins purified and characterized as allergens by in vitro and in vivo assays. Three isoforms, belonging to the TLP family, were purified by different chromatographic systems and characterized by N -terminal amino acid sequences, molecular weight determination (MALDI) and enzymatic activity analysis (,-1,3-gluconase test and inhibition growth of fungi). In the same way, their IgE-binding capacity and allergenic activity were tested by ELISA assays, basophil activation tests and skin prick tests (SPT). Results Two peach-TLPs, Pru p 2.0101 and Pru p 2.0201, were identified as IgE-binding spots by 2D electrophoresis. Another peach-TLP, Pru p 2.0301, was cloned and produced as recombinant protein in a yeast system. The three isoforms were purified and characterized as TLPs by immunoblotting with anti-chestnut TLP antibodies and anti-plant N -asparagine complex glycan (anti-cross-reactive carbohydrate determinant). All of them showed ,-1,3-glucanase activity and inhibition of fungal growth. The three TLPs were recognized by around 50% of the sera from 31 patients analysed in ELISA experiments. All three gave a positive response to an SPT and/or in basophil activation experiments. Conclusion Three isoforms, belonging to the TLP family, were identified in peach as principal allergens. Their prevalence, observed in in vitro, ex vivo and in vivo analyses, suggests that they are important allergens and should therefore be included in the routine diagnosis of peach allergy, at least in the Mediterranean area. Cite this as: A. Palacín, L. Tordesillas, P. Gamboa, R. Sanchez-Monge, J. Cuesta-Herranz, M. L. Sanz, D. Barber, G. Salcedo and A. Díaz-Perales, Clinical & Experimental Allergy, 2010 (40) 1422,1430. [source] Characterization of Bet v 1-related allergens from kiwifruit relevant for patients with combined kiwifruit and birch pollen allergyMOLECULAR NUTRITION & FOOD RESEARCH (FORMERLY NAHRUNG/FOOD), Issue S2 2008Christina Oberhuber Abstract Allergy to kiwifruit appears to have become more common in Europe and elsewhere during the past several years. Seven allergens have been identified from kiwifruit so far, with actinidin, kiwellin and the thaumatin-like protein as the most relevant ones. In contrast to other fruits, no Bet v 1 homologues were characterized from kiwifruit so far. We cloned, purified, and characterized recombinant Bet v 1-homologous allergens from green (Actinidia deliciosa, Act d 8) and gold (Actinidia chinensis, Act c 8) kiwifruit, and confirmed the presence of its natural counterpart by inhibition assays. Well-characterized recombinant Act d 8 and Act c 8 were recognized by birch pollen/kiwifruit (confirmed by double-blind placebo-controlled food challenge) allergic patients in IgE immunoblots and ELISA experiments. The present data point out that Bet v 1 homologues are allergens in kiwifruit and of relevance for patients sensitized to tree pollen and kiwifruit, and might have been neglected so far due to low abundance in the conventional extracts used for diagnosis. [source] Proteomic analysis of bacterial-blight defense-responsive proteins in rice leaf bladesPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 22 2006Tariq Mahmood Abstract Plants exhibit resistance against incompatible pathogens, via localized and systemic responses as part of an integrated defense mechanism. To study the compatible and incompatible interactions between rice and bacteria, a proteomic approach was applied. Rice cv. Java 14 seedlings were inoculated with compatible (Xo7435) and incompatible (T7174) races of Xanthomonasoryzae pv. oryzae (Xoo). Cytosolic and membrane proteins were fractionated from the leaf blades and separated by 2-D PAGE. From 366 proteins analyzed, 20 were differentially expressed in response to bacterial inoculation. These proteins were categorized into classes related to energy (30%), metabolism (20%), and defense (20%). Among the 20 proteins, ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit (RuBisCO LSU) was fragmented into two smaller proteins by T7174 and Xo7435 inoculation. Treatment with jasmonic acid (JA), a signaling molecule in plant defense responses, changed the level of protein accumulation for 5 of the 20 proteins. Thaumatin-like protein and probenazole-inducible protein (PBZ) were commonly up-regulated by T7174 and Xo7435 inoculation and JA treatment. These results suggest that synthesis of the defense-related thaumatin-like protein and PBZ are stimulated by JA in the defense response pathway of rice against bacterial blight. [source] Crystallization and preliminary X-ray diffraction studies of NP24-I, an isoform of a thaumatin-like protein from ripe tomato fruitsACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2005Raka Ghosh NP24 is a 24,kDa (207-amino-acid) antifungal thaumatin-like protein (TLP) found in tomato fruits. An isoform of the protein, NP24-I, is reported to play a possible role in ripening of the fruit in addition to its antifungal properties. The protein has been isolated and purified and crystallized by the hanging-drop vapour-diffusion method. The crystals belong to the tetragonal space group P43, with unit-cell parameters a = b = 61.01, c = 62.90,Å and one molecule per asymmetric unit. X-ray diffraction data were processed to a resolution of 2.45,Å and the structure was solved by molecular replacement. [source] Molecular biology of grape berry ripeningAUSTRALIAN JOURNAL OF GRAPE AND WINE RESEARCH, Issue 2 2000SIMON P. ROBINSON Abstract Grapevines produce non-climacteric fruit that exhibit a double sigmoidal pattern of growth. Ripening occurs during the second growth phase when grapes change colour, start to soften, accumulate reducing sugars, metabolise organic acids and synthesise flavour compounds. Unlike many other fruit, grapes ripen while the berries are still expanding, and as with most non-climacteric fruit, ripening does not appear to be controlled by ethylene. Sugars and amino acids that accumulate in grapes during ripening are imported via the phloem, while many secondary metabolites are synthesised within the berry itself. Grapes import sucrose but accumulate hexoses. Conversion of sucrose to hexoses is most likely catalysed by invertase. cDNAs encoding vacuolar invertases have been isolated from grape berries. Expression of these genes and an increase in invertase activity occur before veraison, so it seems unlikely that synthesis of this enzyme is a controlling factor for sugar accumulation during ripening. Proteins that transport sugars into the berry vacuole may regulate sugar accumulation, and cDNAs encoding both sucrose and hexose transporters have been isolated from ripening grape berries. Determination of the role of these transporters may reveal the pathway of sugar accumulation in grapes. Anthocyanins are only synthesised in the skin of red grapes after veraison. Analysis of the patterns of expression of genes in the flavonoid pathway has shown that there is a dramatic increase in expression of many of these genes in skin cells at veraison. Expression of the gene encoding a glycosyl transferase involved in the lasts steps of anthocyanin synthesis was absolutely correlated with anthocyanin synthesis and may explain the lack of anthocyanin synthesis in white grapes and in the flesh of most red grapes. We infer that the synthesis of anthocyanins is regulated at the transcription level and is likely to be controlled by regulatory genes. Softening of fruit generally results from changes in the properties of cell walls. Analysis of the cell walls of grapes during ripening suggests that there are no dramatic changes in polysaccharide composition but modification of specific components may contribute to softening. A number of proteins are newly synthesised in grapes during ripening and several of these proteins have now been identified. The most abundant are pathogenesis-related (PR) proteins, including chitinases and thaumatin-like proteins. Expression of genes encoding a number of PR proteins increased dramatically in grapes during ripening. It is not clear what role the PR proteins play during ripening but they may provide resistance to pathogens. Differential screening of a post-veraison grape berry cDNA library has also identified ripening-related genes, some of which encode proline-rich cell wall proteins. Other grape ripening-related genes have homologues that are induced by stress in other plants. These studies indicate that a dramatic change in gene expression occurs in grape berries at veraison and suggest that ripening involves a coordinated increase in transcription of a number of different genes. [source] Characterization of peach thaumatin-like proteins and their identification as major peach allergensCLINICAL & EXPERIMENTAL ALLERGY, Issue 9 2010A. Palacín Summary Background Peach is the most important fruit related to food allergy in the Mediterranean area. Pru p 3, its lipid transfer protein, has been described as the principal allergen responsible for cross-reactivities with other foods and pollen and the severity of clinical symptoms. However, the involvement of other allergenic families cannot be ruled out. Thaumatin-like proteins (TLPs) have been described as food allergen in several fruits, such as apple, cherry, kiwi and banana, and pollen. Objective To identify members of the TLP family in peach fruit and to characterize putative allergens. Methods Through two-dimensional (2D) electrophoresis of peach extract and immunodetections with a pool of peach-allergic patients, IgE-binding spots were identified and the corresponding proteins purified and characterized as allergens by in vitro and in vivo assays. Three isoforms, belonging to the TLP family, were purified by different chromatographic systems and characterized by N -terminal amino acid sequences, molecular weight determination (MALDI) and enzymatic activity analysis (,-1,3-gluconase test and inhibition growth of fungi). In the same way, their IgE-binding capacity and allergenic activity were tested by ELISA assays, basophil activation tests and skin prick tests (SPT). Results Two peach-TLPs, Pru p 2.0101 and Pru p 2.0201, were identified as IgE-binding spots by 2D electrophoresis. Another peach-TLP, Pru p 2.0301, was cloned and produced as recombinant protein in a yeast system. The three isoforms were purified and characterized as TLPs by immunoblotting with anti-chestnut TLP antibodies and anti-plant N -asparagine complex glycan (anti-cross-reactive carbohydrate determinant). All of them showed ,-1,3-glucanase activity and inhibition of fungal growth. The three TLPs were recognized by around 50% of the sera from 31 patients analysed in ELISA experiments. All three gave a positive response to an SPT and/or in basophil activation experiments. Conclusion Three isoforms, belonging to the TLP family, were identified in peach as principal allergens. Their prevalence, observed in in vitro, ex vivo and in vivo analyses, suggests that they are important allergens and should therefore be included in the routine diagnosis of peach allergy, at least in the Mediterranean area. Cite this as: A. Palacín, L. Tordesillas, P. Gamboa, R. Sanchez-Monge, J. Cuesta-Herranz, M. L. Sanz, D. Barber, G. Salcedo and A. Díaz-Perales, Clinical & Experimental Allergy, 2010 (40) 1422,1430. [source] | |||||||||||||