actinidin/hypersensitivity

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Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy.

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Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with

Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein.

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Kiwifruit is a significant elicitor of allergy both in children and adults. Digestibility of two kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), was assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of

IgE sensitization profiles toward green and gold kiwifruits differ among patients allergic to kiwifruit from 3 European countries.

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BACKGROUND Kiwifruits have become a major elicitor of plant food allergy. Until recently, the only species of kiwifruit grown commercially was the common green-fleshed Actinidia deliciosa cv Hayward. In 1999, the yellow-fleshed cultivar Actinidia chinensis cv Hort16A was introduced into the

Kiwifruit allergies.

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While kiwifruit has a high nutritive and health value, a small proportion of the world's population appears to be allergic to the fruit. IgE-mediated kiwifruit allergy is often associated with birch and grass pollinosis as well as with latex allergy. Isolated allergy to kiwifruit is also relatively

Allergy to kiwi in patients with baker's asthma: identification of potential cross-reactive allergens.

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BACKGROUND Baker's asthma is a frequent IgE-mediated occupational disorder mainly provoked by inhalation of cereal flour. Allergy to kiwifruit has being increasingly reported in the past few years. No association between both allergic disorders has been described so far. METHODS Twenty patients with

Actinidin, a protease from kiwifruit, induces changes in morphology and adhesion of T84 intestinal epithelial cells.

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Actinidin belongs to the papain-like family of cysteine proteases and is a major kiwifruit allergen. In this study, the effect of actinidin on cellular morphology and adhesion of T84 intestinal cells was investigated. Both rounding and detachment of T84 cells were observed upon actinidin treatment.

The effect of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells.

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Actinidin, a kiwifruit cysteine protease, is a marker allergen for genuine sensitization to this food allergen source. Inhalatory cysteine proteases have the capacity for disruption of tight junctions (TJs) enhancing the permeability of the bronchial epithelium. No such properties have been reported

Identification of actinidin as the major allergen of kiwi fruit.

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BACKGROUND Allergic reactions to fruits and vegetables are among the most frequent food allergies in adults. Kiwi fruit (Actinidia chinensis) is commonly involved, causing local mucosal, systemic, or both types of symptoms by an IgE-mediated mechanism. In a previous study on 30 patients allergic to

Diversity and relative levels of actinidin, kiwellin, and thaumatin-like allergens in 15 varieties of kiwifruit (Actinidia).

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In the last 30 years the incidence of kiwifruit allergy has increased with the three major allergenic proteins being identified as actinidin, kiwellin, and thaumatin-like protein (TLP). We report wide variation in the levels of actinidin and TLP in 15 kiwifruit varieties from the four most widely

Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions.

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BACKGROUND The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease--actinidin (Act d1) on the integrity of intestinal epithelium tight junctions

Crystal structure of kiwellin, a major cell-wall protein from kiwifruit.

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Kiwellin is a cysteine-rich, cell wall-associated protein with no known structural homologues. It is one of the most abundant proteins in kiwifruit (Actinidia spp.), and has been shown to be recognised by IgE of some patients allergic to kiwifruit. Cleavage of kiwellin into an N-terminal 4 kDa

The Kiwifruit Allergen Act d 1 Activates NF-κB Signaling and Affects mRNA Expression of TJ Proteins and Innate Pro-Allergenic Cytokines.

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Impairment of the intestinal barrier is one of the key events in the initiation of the sensitization process in food allergy. The aim of this study was to explore the effects of kiwifruit allergen Act d 1 on intestinal permeability and tight junction protein (TJP) gene expression in vivo and to

Immunoglobulin E recognition patterns to purified Kiwifruit (Actinidinia deliciosa) allergens in patients sensitized to Kiwi with different clinical symptoms.

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BACKGROUND Green kiwifruit allergy is on the rise. However, no surveys testing purified major kiwi allergens have been carried out in a large population, including both kiwi-sensitized [skin prick test (SPT)-positive] and truly kiwi-allergic patients. OBJECTIVE To isolate major kiwifruit allergens,

Comparative molecular modelling identifies a common putative IgE epitope on cysteine protease allergens of diverse sources.

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BACKGROUND Previous approaches for studying common allergenic epitopes have mainly focused on sequence comparisons, which unfortunately yield little or no information on the shape of the epitope which is the most important determinant of cross-reactivity. OBJECTIVE The aim of this study was to

Molecular characterization of allergens in raw and processed kiwifruit.

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BACKGROUND The prevalence of allergy to kiwifruit is increasing in Europe since the last two decades. Different proteins have been identified as kiwifruit allergens; even though with geographic differences, Act d 1, a cysteine protease protein of 30 kDa, and Act d 2, a thaumatin-like protein of 24

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