M. Villalba et al., THE AMINO-ACID-SEQUENCE OF OLE-E I, THE MAJOR ALLERGEN FROM OLIVE TREE (OLEA-EUROPAEA) POLLEN, European journal of biochemistry, 216(3), 1993, pp. 863-869
The complete primary structure of the major allergen from Olea europae
a (olive tree) pollen, Ole e I (IUIS nomenclature), has been determine
d. The amino acid sequence was established by automated Edman degradat
ion of the reduced and alkylated molecule as well as of selected fragm
ents obtained by proteolytic digestions. Ole e I contains a single pol
ypeptide chain of 145 amino acid residues with a calculated molecular
mass of 16331 Da. No free sulfhydryl groups have been detected in the
native protein. The molecule contains a putative glycosylation site. A
high degree of microheterogeneity has been observed, mainly centered
in the first 33% of the molecule. Comparison of Ole e I sequence with
protein sequence databases showed no similarity with other known aller
gens. However, it has a 36% and 38% sequence identity with the putativ
e polypeptide structures, deduced, respectively, from nucleotide seque
nces of genes isolated from tomato anthers and com pollen, which have
been suggested to be involved in the growing of the pollen tube. There
fore, the olive tree allergen may be a constitutive protein of the pol
len involved in reproductive functions.