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J. Biol. Chem., Vol. 279, Issue 37, 39035-39041, September 10, 2004

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NMR Solution Structure of Ole e 6, a Major Allergen from Olive Tree Pollen^*

Miguel Ángel Treviño, María Flor García-Mayoral, Patricia Barral¶||, Mayte Villalba¶, Jorge Santoro, Manuel Rico, Rosalía Rodríguez¶, and Marta Bruix**

From the Departamento de Espectroscopía y Estructura Molecular, Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Serrano 119, 28006 Madrid, Spain and the ^¶Departamento de Bioquímica y Biología Molecular I, Facultad de Química, Universidad Complutense, 28040 Madrid, Spain

Ole e 6 is a pollen protein from the olive tree (Olea europaea) that exhibits allergenic activity with a high prevalence among olive-allergic individuals. The three-dimensional structure of Ole e 6 has been determined in solution by NMR methods. This is the first experimentally determined structure of an olive tree pollen allergen. The structure of this 50-residue protein is based on 486 upper limit distance constraints derived from nuclear Overhauser effects and 24 torsion angle restraints. The global fold of Ole e 6 consists of two nearly antiparallel -helices, spanning residues 3-19 and 23-33, that are connected by a short loop and followed by a long, unstructured C-terminal tail. Viewed edge-on, the structured N terminus has a dumbbell-like shape with the two helices on the outside and with the hydrophobic core, mainly composed of 3 aromatic and 6 cysteine residues, on the inside. All the aromatic rings lie on top of and pack against the three disulfide bonds. The lack of thermal unfolding, even at 85 °C, indicates a high conformational stability. Based on the analysis of the molecular surface, we propose five plausible epitopes for IgE recognition. The results presented here provide the structural foundation for future experiments to verify the antigenicity of the proposed epitopes, as well as to design novel hypoallergenic forms of the protein suitable for diagnosis and treatment of type-I allergies. In addition, three-dimensional structure features of Ole e 6 are discussed to provide a basis for future functional studies.

Received for publication, June 1, 2004 , and in revised form, June 30, 2004.

The atomic coordinates and structure factors (code 1SS3) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by Grant CAM2002-07B/0054 from the Comunidad Autónoma de Madrid and Grant SAF2002-02711 from the Ministerio de Ciencia y Tecnología (Spain). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipients of fellowships from the Comunidad Autónoma de Madrid (CAM, Spain).

^|| Recipient of a fellowship from the Ministerio de Educación, Cultura y Deporte (Spain).

^** To whom correspondence should be addressed. Fax: 34-91-561-94-00; E-mail: mbruix{at}iqfr.csic.es.

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