Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity
Autor: | Annick Barre, Raphaël Culerrier, Claude Granier, Pierre Rougé, Jean-Philippe Borges, Alain Didier |
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Rok vydání: | 2008 |
Předmět: |
Rosaceae
Biophysics Cross Reactions medicine.disease_cause Immunoglobulin E Biochemistry Cross-reactivity Ige binding Epitope Epitopes Allergen Consensus Sequence medicine Animals Humans Molecular Biology Plant Proteins biology Chemistry Cell Biology Allergens Antigens Plant biology.organism_classification Epitope mapping Fruit biology.protein Rabbits Carrier Proteins Plant lipid transfer proteins Protein Binding |
Zdroj: | Biochemical and Biophysical Research Communications. 365:685-690 |
ISSN: | 0006-291X |
DOI: | 10.1016/j.bbrc.2007.11.046 |
Popis: | Four IgE-binding epitopes have been characterized that cover a large area (⩾40%) of the molecular surface of lipid transfer protein allergens of Rosaceae (apple, peach, apricot, and plum). They mainly correspond to electropositively charged regions protruding on the molecular surface of the modeled apple (Mal d 3), apricot (Pru ar 3), and plum (Pru d 3) allergens. Two of these epitopes consist of consensus epitopes structurally conserved among the lipid transfer protein allergens from the Rosaceae. Their occurrence in different lipid transfer protein allergens presumably accounts for the IgE-binding cross-reactivity often observed among different Rosaceae fruits. In this respect, LTP consist of phylogenetically- and structurally-related pan allergens. However, the IgE-binding cross-reactivity due to fruit lipid transfer protein has varying degrees of clinical relevance and this cross-reactivity is not necessarily accompanied by a cross-allergenicity to the corresponding fruits. |
Databáze: | OpenAIRE |
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