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The Journal of Immunology, 2004, 172: 3644-3651.
Copyright © 2004 by The American Association of Immunologists

A Major Allergen from Pollen Defines a Novel Family of Plant Proteins and Shows Intra- and Interspecie Cross-Reactivity1

Patricia Barral*, Eva Batanero*, Oscar Palomares*, Joaquín Quiralte{dagger}, Mayte Villalba* and Rosalía Rodríguez*,2

* Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid, Spain; and {dagger} Unidad de Alergia, Complejo Hospitalario de Jaén, Jaén, Spain

Olive tree (Olea europaea) pollen is a main cause of allergy associated with extensive areas of Europe and North America. Ole e 10, a small (10.8 kDa) and acidic (pI 5.8) protein, has been identified as a major allergen from the olive pollen, isolated, and characterized. Circular dichroism analysis gave 17% {alpha} helix, 33% {beta} sheet, and 21% {beta} turn for its secondary structure. Based on amino acid sequences of tryptic peptides, the protein was cloned and sequenced. The allergen consists of a single polypeptide chain of 102 aa, with a signal peptide of 21 residues. Ole e 10 showed homology with the C-terminal domain of another olive allergen, Ole e 9 (1,3-{beta}-glucanase, 53% identity), with deduced sequences from Arabidopsis thaliana genes (42–46% identity) and with polypeptide segments (Cys boxes) of proteins involved in yeast development (Epd1/Gas-1p/Phr2 families; 42–43% similarity). Ole e 10 showed 55% prevalence for olive-allergic patients and exhibited an IgE response dependent on its conformation. Remarkable IgE cross-reactivity was detected with Ole e 9, but no correlation was observed between the individual IgE responses to both allergens. Ole e 10 shares IgE B cell epitopes with proteins from Oleaceae, Gramineae, Betulaceae, Chenopodiaceae, Cupressaceae, Ambrosia, and Parietaria pollens, latex, and vegetable foods, such as tomato, kiwi, potato, and peach. These data indicate that Ole e 10 is a new pan-allergenic plant protein that shows notable intra- and interspecie IgE cross-reactivity and is a powerful candidate to be involved in pollen-latex-fruit syndrome.




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M. A. Trevino, O. Palomares, I. Castrillo, M. Villalba, R. Rodriguez, M. Rico, J. Santoro, and M. Bruix
Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen
Protein Sci., February 1, 2008; 17(2): 371 - 376.
[Abstract] [Full Text] [PDF]


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M. A. Trevino, M. F. Garcia-Mayoral, P. Barral, M. Villalba, J. Santoro, M. Rico, R. Rodriguez, and M. Bruix
NMR Solution Structure of Ole e 6, a Major Allergen from Olive Tree Pollen
J. Biol. Chem., September 10, 2004; 279(37): 39035 - 39041.
[Abstract] [Full Text] [PDF]




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