Analysis of the heat stability of lipid transfer protein from apple
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Pepsin
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The role of an allergist in recognizing the pollen-food allergy syndrome (PFAS) and lipid transfer protein syndrome (LTPS) is essential. LTPS differs from PFAS by having a different family of panallergens and clinical characteristics. Both are complex syndromes posing diagnostic and therapeutic challenges. Many cross-reactive allergen components are involved, such as plant panallergens profilins, PR-10 proteins (Bet v 1 homologous), and lipid transfer proteins (LTP). PFAS results from cross-reactivity between pollen-specific immunoglobulin E (IgE) and homologous proteins found in fruits and vegetables. In most cases, grass pollen is responsible for profilin hypersensitivity. But, tree and weed pollen may also act as primary sensitizers, depending on geographical differences. Nonspecific LTP (nsLTP) is ubiquitous in terrestrial plants and can induce systemic allergic severe reactions. Peach (Pru P 3) is the primary sensitizer for LTP-driven allergy, and its clinical relevance is considered the prototypic marker for LTPS. nsLTPs have been identified as a major allergen in tree and weed plants. A second critical point is the diagnosis of LTPS associated with cofactors such as exercise, alcohol, antacids, and NSAIDS, that can promote severe reactions. Skin Prick Test (SPT) with Peach extracts that have been highly enriched for Pru p 3 with very low content of other allergens for LTPS, is suggestive of LTPS. For PFAS, positive SPT with profilin-enriched date palm pollen and watermelon extract shows sensitivity and specificity that is very close to that of the recombinant grass pollen profilin. The present review address differences between the PFAS from LTP syndrome with particular attention to the clinical impact on cross-reactivity or cross-sensitization to pollens.
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Profilin
Cross-reactivity
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Food allergens
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Vegetable Proteins
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744 Background: Cereals are the most important nutritional component in the human diet. Food-induced allergic reactions to these substances therefore have serious implications, and exhaustive diagnosis is required. Such diagnosis is still difficult because of the incomplete knowledge about major cereal allergens. In particular, few food-induced allergic reactions to maize have been reported, and no information on the allergenic proteins is available. Objective: Having observed several anaphylactic reactions to maize, we planned a study to identify maize major allergens and cross-reactivity with other cereals, as well as to peach because the majority of patients also reacted to Prunoideae fruits. Methods: Twenty-two patients with systemic symptoms after maize ingestion and positive skin prick test responses and serum-specific IgE antibodies to maize were selected. The IgEreactivity pattern was identified by SDS-PAGE and immunoblotting. The major allergen identified was then purified by HPLC and characterized by mass spectrometry, determination of the isoelectric point value, and N-terminal amino acid sequencing. Results: Sera from 19 (86%) of the 22 patients recognized a 9kd protein, thus confirming this as the maize major allergen. This protein had an isoelectric point of greater than 9, a molecular mass of 9047.0 d, and no glycosylation. Determination of its N-terminal sequence showed that it was a lipid transfer protein (LTP). By using immunoblotting-inhibition experiments, we demonstrated that the LTP cross-reacts completely with rice and peach LTPs but not with wheat or barley LTPs. N-terminal sequence of the 16-kd allergen (recognized by 36% of patients) showed it to be the maize inhibitor of trypsin. This protein cross-reacts completely with grass, wheat, barley, and rice trypsin inhibitors. Conclusion: The major allergen of maize is an LTP with a molecular weight of 9 kd that is highly homologous with the peach LTP, the major allergen of the Prunoideae subfamily. (J Allergy Clin Immunol 2000;106:744-51.) Cereal grains belong to the Gramineae botanical family, which is a well-known cause of allergic and immunologic reactions. Cereals include important crops, such as wheat, barley, rye, oats, rice, and maize, and are thus the major components of the human diet throughout the world. The implications of sensitization to any of these
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Only 2 allergenic proteins have been described in lettuce allergy: a 16-kDa protein (putative profilin) and a lipid transfer protein (LTP) named Lac s 1.
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Basophil activation
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Recent studies show that the lipid transfer protein (LTP), the major Rosaceae allergen in patients not sensitized to birch pollen, is a largely cross-reacting allergen. Moreover, it is a potentially hazardous allergen due to its stability upon thermal treatment and pepsin digestion. The present study reports 3 cases of rice-induced anaphylaxis in LTP-allergic patients. In vitro inhibition studies, carried out using LTP purified from both rice and apple as well as whole peach extract, show that LTP was the relevant allergen in these patients and demonstrate the cross-reactivity between rice LTP and peach/apple LTP.
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Peach-induced contact urticaria is frequent in peach-allergic subjects.It was the aim of this study to detect whether contact urticaria is associated with a specific peach allergen.Ninety-two peach-allergic subjects were studied. Patients were diagnosed as being sensitized to lipid transfer protein (LTP; Pru p 3) or as having a pollen-food allergy syndrome induced by Pru p 1 and/or profilin, Pru p 4, on the basis of the results of a skin prick test containing these allergenic proteins in an isolated form. Specific IgE to peach extract was measured as well. Contact urticaria was confirmed by a contact test with intact, untreated peach. A contact test with nectarine was carried out as control.Overall, contact urticaria was present in 21% of patients; the peach contact test scored positive in all cases. Contact urticaria was significantly more frequent in patients hypersensitive to LTP (63%) than in subjects with pollen-food allergy syndrome (6%; p < 0.001) and was not associated with a higher level of peach-specific IgE. In several cases, contact urticaria preceded the onset of food allergy by years. The contact test with nectarine scored negative in 5/5 cases.Although the peach contact test was not performed in all subjects, and peach allergy was not confirmed by oral challenges, this study shows that peach-induced contact urticaria is associated with sensitization to peach LTP. The negative clinical history and contact test with nectarine along with the well-known high concentration of LTP in peach fuzz suggest that peach fuzz plays a role in the pathogenesis of contact urticaria.
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