Latex-fruit syndrome

Servicio de Alergología. Hospital Doctor Negrín. Las Palmas de Gran Canaria. Spain.
Allergologia et Immunopathologia (Impact Factor: 1.74). 01/2002; 30(3):156-63.
Source: PubMed


During the last decade, latex IgE-mediated allergy has been recognized as a very important medical problem. At the same time, many studies have dealt with allergic cross-reactions between aeroallergens and foods. In this context, there is clear evidence now on the existence of significant clinical association between latex and fruit allergies. Therefore, a latex-fruit syndrome has been postulated.Several studies have demonstrated that from 20% to 60% of latex-allergic patients show IgE-mediated reactions to a wide variety of foods, mainly fruits. Although implicated foods vary among the studies, banana, avocado, chestnut and kiwi are the most frequently involved. Clinical manifestations of these reactions may vary from oral allergy syndrome to severe anaphylactic reactions, which are not uncommon, thus remarking the clinical relevance of this syndrome.The diagnosis of food hypersensitivities associated to latex allergy is based on the clinical history of immediate adverse reactions, suggestive of an IgE-mediated sensitivity. Prick by prick test with the fresh foods implicated in the reactions shows an 80% concordance with the clinical diagnosis, and therefore it seems to be the best diagnostic test available nowadays in order to confirm the suspicion of latex-fruit allergy. Once the diagnosis is achieved, a diet free of the offending fruits is mandatory.Recently, some of the common allergens responsible for the cross-reactions among latex and the fruits most commonly implicated in the syndrome have been identified. Class I chitinases, with an N-terminal hevein like domain, which cross-react with the major latex allergen hevein, seem to be the panallergens responsible for the latex-fruit syndrome.

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    • "c o m / l o c a t e / f o o d c h e m These homologies can cause cross-reactions that usually occur in related molecular species of the same family, for example lentils and peas (Martínez San Ireneo, Ibáñez, Fernández-Caldas, & Carnés, 2008). However, cross-reactivity between members of different botanical families have also been reported, such as in the latexfruit syndrome (Blanco, 2003). "
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    ABSTRACT: IgE-mediated reactions to food allergens constitute a major health problem in industrialized countries. Chickpea is consumed in Mediterranean countries, and reportedly associated with IgE-mediated hypersensitivity reactions. However, the nature of allergic reactions to chickpea has not been characterized. A serum pool from paediatric patients allergic to chickpeas was used to detect IgE-binding proteins from chickpea seeds by immunoassay and immunoblot inhibition assay. Protein samples enriched in chickpea legumin and vicilin were obtained by anion exchange chromatography, and were identified by mass spectrometric analysis. IgE-immunoassays of globulin fractions from chickpeas revealed that vicilin (50kDa) and the basic subunit of legumin (20kDa) were bound by IgE from patient sera. Pea and lentil protein extracts strongly inhibited the IgE binding to chickpea globulin. We speculate that vicilin and the basic subunit of legumin are major chickpea allergens. Also, the globulin fraction of chickpea likely cross-reacts with the allergenic proteins of pea and lentil.
    Food Chemistry 05/2013; 138(1):13-8. DOI:10.1016/j.foodchem.2012.10.031 · 3.39 Impact Factor
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    • "Several analyses of different plant-derived food allergens have also shown the presence of this polypeptide chain as a chitin-binding domain in class I endochitinases . This accounts for the cross-reactivity between latex and some fruits (Blanco, 2003). The first mapping of the linear epitopes of Hev b 6.02, using overlapping peptides in direct or inhibition ELISA was performed by Beezhold et al. (1997) and Banerjee et al. (1997). "
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    ABSTRACT: Hev b 6.02 (hevein), identified as a major allergen from natural rubber latex (NRL), is involved in the latex-fruit syndrome and also acts as a pathogenesis defense-related protein. Its 3D structure has been solved at high resolution, and its linear epitopes have already been reported. However, information about conformational epitopes is still controversial, even though it is relevant for an accurate diagnosis and treatment, as well as for the study of allergen–antibody molecular interactions. We sought to analyze the B-cell epitopes of Hev b 6.02 at a molecular and structural level, using specific recombinant antibodies. We obtained a murine monoclonal antibody (mAb 6E7) and three human single chain fragments (scFvs A6, H8, and G7) anti-Hev b 6.02 that were able to compete for hevein binding with serum IgEs from latex allergic patients. In vitro assays showed that the mAb 6E7 and scFv H8 recognized the area of Hev b 6.02 where the aromatic residues are exposed; while the scFv G7 defined the amino and carboxy-terminal regions that lie close to each other, as a different epitope. The structural modeling of the Hev b 6.02–scFv H8 and Hev b 6.02–scFv G7 complexes revealed the putative regions of two conformational epitopes. In one of these, the aromatic residues, as well as polar side chains are important for the interaction, suggesting that they are part of a dominant conformational epitope also presented on the Hev b 6.02–IgE interactions. Antibodies recognizing this important allergen have potential to be used to diagnose and ultimately treat latex allergy.
    Molecular Immunology 02/2009; 46(4-46):668-676. DOI:10.1016/j.molimm.2008.08.282 · 2.97 Impact Factor
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    ABSTRACT: The occurrence of homologous proteins in foods, pollen and latex is the molecular basis of the plant sources' allergenic cross-reactivity. However, there is not a generic cross-reactivity. Each allergic patient is sensitized to particular allergens and even to particular IgE-binding epitopes. Molecular studies on the main panallergens may explain the major plant-food, pollen and latex syndromes. Some examples of the best- characterized plant panallergens are presented. Novel technologies on recombinant proteins and microarrayed allergens will provide allergen-sensitization profiles, associated to food allergies and cross-reactivity, that will enable the diagnosis and prediction of cross-reactions as well as individual treatment of these pathologies.
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