ArticleMolecular immunology2011
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.
Article in Molecular immunology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 55 citations in OpenAlex.
- Purification and Characterization of Punein, a Pomegranate PR-4 Protein Showing Structural Similarities with the Hevein Precursor.Molecules (Basel, Switzerland) · 2025Article
- Revisiting Latex-Fruit Syndrome after 30 Years of Research: A Comprehensive Literature Review and Description of Two Cases.Journal of clinical medicine · 2024Review
- Latex Allergy in Children.Journal of clinical medicine · 2023Review
- Revisiting Fruit Allergy: Prevalence across the Globe, Diagnosis, and Current Management.Foods (Basel, Switzerland) · 2023Review
- Molecular approach to a patient's tailored diagnosis of the oral allergy syndrome.Clinical and translational allergy · 2020Review
- Component-Resolved Diagnosis in Food Allergies.Medicina (Kaunas, Lithuania) · 2019Review
- Latex hypersensitivity among allergic Egyptian children: relation to parental/self reports.Pulmonary medicine · 2014Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
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 the extent of cross-reactivity between hevein and HLDs using sera from latex-allergic patients with and without plant food allergy. Hevein and HLDs of latex, banana, and avocado chitinases were expressed in Escherichia coli as fusion proteins with the maltose-binding protein and purified by affinity chromatography. IgE binding to these proteins was studied in sera from 59 latex-allergic patients and 20 banana-allergic patients without latex allergy by ELISA and ELISA inhibition. Additionally, 16,408 allergic patients' sera were tested for IgE binding to hevein, latex chitinase, and wheat germ agglutinin using an allergen microarray. Hevein-specific IgE was detected in 34/59 (58%) latex-allergic patients' sera. HLDs of latex, banana, and avocado chitinases were recognized by 21 (36%), 20 (34%), and 9 (15%) sera, respectively. In contrast, only one of 20 banana-allergic patients without latex allergy was sensitized to chitinase HLDs. In most tested latex-allergic patients' sera, IgE binding to hevein was only partially reduced by preincubation with HLDs. Among hevein-sensitized, latex-allergic patients, the percentage of plant food allergy (15/34 = 44%) was equal to latex-allergic patients without hevein sensitization (11/25 = 44%). In the general allergic population, 230 of 16,408 sera (1.4%) reacted to hevein and/or a hevein-like allergen. Of these, 128 sera showed an isolated sensitization to hevein, whereas only 17 bound to latex chitinase or wheat germ agglutinin without hevein sensitization. In conclusion, the IgE response to HLDs is elicited by hevein as sensitizing allergen in most cases. Despite considerable cross-reactivity between these allergens, no correlation between latex-associated plant food allergy and sensitization to hevein or HLDs was found.
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