| Class I chitinases as potential panallergens involved in the latex-fruit syndrome. | |
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MedLine Citation:
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PMID: 10069887 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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BACKGROUND: Latex-fruit cross-sensitization has been fully demonstrated. However, the antigens responsible for this "latex-fruit syndrome" have not been identified. We have recently shown that class I chitinases are relevant chestnut and avocado allergens. OBJECTIVE: We sought to evaluate the in vivo and in vitro reactions of purified chestnut and avocado chitinases in relation to the latex-fruit syndrome. METHODS: From a latex-allergic population, eighteen patients allergic to chestnut, avocado, or both were selected. Skin prick tests (SPTs) were performed with crude chestnut and avocado extracts, chitinase-enriched preparations, and purified class I and II chitinases from both fruits. CAP-inhibition assays with the crude extracts and purified proteins were carried out. Immunodetection with sera from patients with latex-fruit allergy and immunoblot inhibition tests with a latex extract were also performed. Eighteen subjects paired with our patients and 15 patients allergic to latex but not food were used as control groups. RESULTS: The chestnut class I chitinase elicited positive SPT responses in 13 of 18 patients with latex-fruit allergy (72%), and the avocado class I chitinase elicited positive responses in 12 of 18 (67%) similarly allergic patients. By contrast, class II enzymes without a hevein-like domain did not show SPT responses in the same patient group. Each isolated class I chitinase reached inhibition values higher than 85% in CAP inhibition assays against the corresponding food extract in solid phase. Immunodetection of the crude extracts and the purified class I chitinases revealed a single 32-kd band for both chestnut and avocado. Preincubation with a natural latex extract fully inhibited the IgE binding to the crude extracts, as well as to the purified chestnut and avocado class I chitinases. CONCLUSION: Chestnut and avocado class I chitinases with an N-terminal hevein-like domain are major allergens that cross-react with latex. Therefore they are probably the panallergens responsible for the latex-fruit syndrome. |
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Authors:
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C Blanco; A Diaz-Perales; C Collada; R Sánchez-Monge; C Aragoncillo; R Castillo; N Ortega; M Alvarez; T Carrillo; G Salcedo |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Journal of allergy and clinical immunology Volume: 103 ISSN: 0091-6749 ISO Abbreviation: J. Allergy Clin. Immunol. Publication Date: 1999 Mar |
Date Detail:
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Created Date: 1999-04-02 Completed Date: 1999-04-02 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 1275002 Medline TA: J Allergy Clin Immunol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 507-13 Citation Subset: AIM; IM |
Affiliation:
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Sección de Alergia, Unidad de Investigación, Hospital Nuestra Señora del Pino, Las Palmas de Gran Canaria, Spain. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adolescent Adult Allergens / adverse effects*, chemistry, immunology Antibody Specificity Antimicrobial Cationic Peptides* Chitinase / adverse effects*, chemistry, classification, immunology Cross Reactions Female Food Hypersensitivity / immunology* Humans Immunoglobulin E / blood, immunology Latex / chemistry Latex Hypersensitivity / immunology* Lauraceae / enzymology, immunology* Lectins / chemistry Male Middle Aged Nuts / enzymology, immunology* Plant Lectins Plant Proteins / adverse effects*, chemistry, classification, immunology Prospective Studies Protein Structure, Tertiary Skin Tests Structure-Activity Relationship |
| Chemical | |
Reg. No./Substance:
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0/Allergens; 0/Antimicrobial Cationic Peptides; 0/Latex; 0/Lectins; 0/Plant Lectins; 0/Plant Proteins; 137295-60-4/hevein; 37341-29-0/Immunoglobulin E; EC 3.2.1.-/Prs a 1 allergen; EC 3.2.1.14/Chitinase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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