Villalba M, Batanero E, López-Otín C, Sánchez L M, Monsalve R I, González de la Peña M A, Lahoz C, Rodríguez R
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Complutense, Madrid, Spain.
Eur J Biochem. 1993 Sep 15;216(3):863-9. doi: 10.1111/j.1432-1033.1993.tb18208.x.
The complete primary structure of the major allergen from Olea europaea (olive tree) pollen, Ole e I (IUIS nomenclature), has been determined. The amino acid sequence was established by automated Edman degradation of the reduced and alkylated molecule as well as of selected fragments obtained by proteolytic digestions. Ole e I contains a single polypeptide 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 allergens. However, it has a 36% and 38% sequence identity with the putative polypeptide structures, deduced, respectively, from nucleotide sequences of genes isolated from tomato anthers and corn pollen, which have been suggested to be involved in the growing of the pollen tube. Therefore, the olive tree allergen may be a constitutive protein of the pollen involved in reproductive functions.
油橄榄（橄榄树）花粉主要变应原Ole e I（国际免疫学会命名法）的完整一级结构已被确定。通过对还原和烷基化分子以及通过蛋白酶消化获得的选定片段进行自动埃德曼降解，确定了氨基酸序列。Ole e I包含一条由145个氨基酸残基组成的单多肽链，计算分子量为16331 Da。在天然蛋白质中未检测到游离巯基。该分子含有一个假定的糖基化位点。观察到高度的微异质性，主要集中在分子的前33%。将Ole e I序列与蛋白质序列数据库进行比较，发现与其他已知变应原没有相似性。然而，它与分别从番茄花药和玉米花粉中分离的基因的核苷酸序列推导的假定多肽结构具有36%和38%的序列同一性，这些基因被认为与花粉管的生长有关。因此，橄榄树变应原可能是参与生殖功能的花粉组成蛋白。
