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Published online before print December 20, 2007, 10.1110/ps.073230008
Protein Science (2008), 17:371-376. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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PROTEIN STRUCTURE REPORT

Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen

Miguel Á. Treviño1, Oscar Palomares2, Inés Castrillo1, Mayte Villalba2, Rosalía Rodríguez2, Manuel Rico1, Jorge Santoro1, and Marta Bruix1

1 Departamento de Espectroscopía y Estructura Molecular, Instituto de Química Física "Rocasolano," CSIC, 28006 Madrid, Spain
2 Departamento de Bioquímica y Biología Molecular I, Facultad de Química, Universidad Complutense, 28040 Madrid, Spain

(RECEIVED September 6, 2007; FINAL REVISION October 25, 2007; ACCEPTED October 31, 2007)

Ole e 9 is an olive pollen allergen belonging to group 2 of pathogenesis-related proteins. The protein is composed of two immunological independent domains: an N-terminal domain (NtD) with 1,3-β-glucanase activity, and a C-terminal domain (CtD) that binds 1,3-β-glucans. We have determined the three-dimensional structure of CtD-Ole e 9 (101 amino acids), which consists of two parallel {alpha}-helices forming an angle of ~55°, a small antiparallel β-sheet with two short strands, and a 3–10 helix turn, all connected by long coil segments, resembling a novel type of folding among allergens. Two regions surrounded by aromatic residues (F49, Y60, F96, Y91 and Y31, H68, Y65, F78) have been localized on the protein surface, and a role for sugar binding is suggested. The epitope mapping of CtD-Ole e 9 shows that B-cell epitopes are mainly located on loops, although some of them are contained in secondary structural elements. Interestingly, the IgG and IgE epitopes are contiguous or overlapped, rather than coincident. The three-dimensional structure of CtD-Ole e 9 might help to understand the underlying mechanism of its biochemical function and to determine possible structure–allergenicity relationships.

Keywords: Ole e 9; allergy; olive pollen; glucanase


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