hevein/hypersensitivity

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HLA class II antigens DR4 and DQ8 are associated with allergy to hevein, a major allergen of Hevea latex.

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In this study we investigated the relationship between HLA class II alleles and the IgE-specific immune response to the 4.7 kDa polypeptide hevein of Hevea brasiliensis, a major latex allergen, 51 individuals with immediate-type latex allergy and 90 controls were examined for the polymorphisms in

Latex-allergic patients sensitized to the major allergen hevein and hevein-like domains of class I chitinases show no increased frequency of latex-associated plant food allergy.

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Allergies to certain fruits such as banana, avocado, chestnut and kiwi are described in 30-70% of latex-allergic patients. This association is attributed to the cross-reactivity between the major latex allergen hevein and hevein-like domains (HLDs) from fruit class I chitinases. We aimed to assess

Class I endochitinase containing a hevein domain is the causative allergen in latex-associated avocado allergy.

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BACKGROUND In the medical literature immunoglobulin (Ig)E-mediated sensitization to avocado is rarely reported. On the other hand, more than 50% of subjects having IgE-mediated natural rubber latex allergy are sensitized to avocado fruit as demonstrated by skin-prick testing and/or specific IgE

Identification of hevein (Hev b 6.02) in Hevea latex as a major cross-reacting allergen with avocado fruit in patients with latex allergy.

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BACKGROUND Recent studies demonstrated that allergy to natural rubber latex is frequently associated with hypersensitivity to avocado fruit. The responsible cross-sensitizing allergen has not been identified. OBJECTIVE The purpose of this study was to investigate the cross-reactivity of a latex

Hevein, an allergenic lectin from rubber latex, activates human neutrophils' oxidative burst.

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Hevein is an N-acetyl-D-glucosamine (GlcNAc) specific lectin that has been hypothesized to participate in the IgE-mediated allergic reactions in patients with latex allergy. In this work we assessed the specificity and biological effect of hevein purified from rubber latex on human leukocytes, using

Isolated hevein-like domains, but not 31-kd endochitinases, are responsible for IgE-mediated in vitro and in vivo reactions in latex-fruit syndrome.

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BACKGROUND Individuals with natural rubber latex allergy often have immediate reactions to plant-derived foods and fresh fruits, such as avocado and banana. IgE of these patients has been shown to bind endochitinases containing an N-terminal hevein-like domain (HLD). However, evidence on 31-kd

The major conformational IgE-binding epitopes of hevein (Hev b6.02) are identified by a novel chimera-based allergen epitope mapping strategy.

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A novel approach to localize and reconstruct conformational IgE-binding epitope regions of hevein (Hev b6.02), a major natural rubber latex allergen, is described. An antimicrobial protein (AMP) from the amaranth Amaranthus caudatus was used as an immunologically non-IgE-binding adaptor molecule to

Differential allergen sensitization patterns in chestnut allergy with or without associated latex-fruit syndrome.

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BACKGROUND Chestnut allergy has been almost exclusively considered in the context of the latex-fruit syndrome. Chestnut allergens not linked to latex hypersensitivity have not been studied. OBJECTIVE We sought to explore whether differences in sensitization patterns between chestnut allergy with or

Class I chitinases with hevein-like domain, but not class II enzymes, are relevant chestnut and avocado allergens.

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BACKGROUND Several foods associated with the latex-fruit syndrome present relevant allergens of around 30 kd. Neither these components nor any other responsible for the reported cross-reactions have been identified and purified. OBJECTIVE We sought to isolate and characterize the 30 kd allergens

Hevein-like protein domains as a possible cause for allergen cross-reactivity between latex and banana.

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BACKGROUND Patients allergic to natural rubber latex (NRL) frequently exhibit immediate hypersensitivity reactions to banana, but the molecular basis of these putative cross-reactions is unknown. OBJECTIVE We wanted to examine whether proteins resembling hevein, a major NRL allergen, exist in banana

Hevein-specific recombinant IgE antibodies from human single-chain antibody phage display libraries.

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IgE antibodies distinctively recognising allergenic epitopes would be ideal reagents in immunodiagnostics to detect and quantify allergens, as well as for the development of allergy diagnostics and therapeutics. We have isolated recombinant human IgE antibodies specific for the major latex allergen,

The hevein domain of the major latex-glove allergen Hev b 6.01 contains dominant T cell reactive sites.

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BACKGROUND Sensitization to natural rubber latex (Hevea brasiliensis) is a major cause of occupational asthma and rhinitis affecting frequent latex-glove users. Hev b 6.01, a known major latex allergen, is cleaved naturally into hevein (4.7 kDa) and a C-terminal fragment (14 kDa). Hevein is an

Isolation and identification of hevein as a major IgE-binding polypeptide in Hevea latex.

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BACKGROUND Polypeptides in Hevea latex are known as the major cause of latex type I sensitivities. So far, only a few of them have been characterized. METHODS Proteins with a molecular weight lower than 10 kd in fresh Hevea latex were separated by ultrafiltration and further characterized by liquid

Sensitization to Ficus benjamina: relationship to natural rubber latex allergy and identification of foods implicated in the Ficus-fruit syndrome.

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BACKGROUND Ornamental Ficus benjamina (FB) has been recognized as a new indoor allergen. Little is known about the prevalence in moderately exposed subjects and the proposed association with fruit and Hevea latex hypersensitivity. OBJECTIVE To study the prevalence of FB sensitization and the

Concomitant sensitization to legumin, Fag e 2 and Fag e 5 predicts buckwheat allergy.

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BACKGROUND Buckwheat (Fagopyrum esculentum) has become increasingly popular as a healthy food in Europe. However, for sensitized individuals, consumption can cause anaphylactic reactions. The aim of this study was to identify individual well-characterized buckwheat allergens for component-resolved

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