Batanero E, Villalba M, Ledesma A, Puente X S, Rodríguez R
Departamento de Bioquímica y Biología Molecular, Facultad de Química, Universidad Complutense, Madrid, Spain.
Eur J Biochem. 1996 Nov 1;241(3):772-8. doi: 10.1111/j.1432-1033.1996.00772.x.
An allergen has been isolated from a saline extract of olive tree (Olea europaea) pollen. The protein consists of a single polypeptide chain of 9.2-kDa, as determined by mass spectrometry. It contains neither tryptophan nor tyrosine residues, and displays an acidic isoelectric point. The secondary structure of the protein, estimated from the analysis of the circular-dichroism spectrum in the peptide-bond region, is composed of 52% alpha-helix, 10% beta-strand, 29% beta-turn and 9% non-regular conformation. The N-terminal end of the protein is blocked. Amino-acid-sequence data have been obtained from peptides produced by CNBr treatment of the native allergen. A partial sequence of 36 amino acids has thus been elucidated. The protein exhibits sequence similarity with pollen allergens from Brassica species and contains a Ca(2+)-binding motif. The isolated protein displays IgE-binding activity against sera of patients allergic to olive-tree pollen. It has been named Ole e 3, according to the recommendations of the IUIS Nomenclature Committee. IgG ELISA inhibition assays with polyclonal antibodies specific for Ole e 3 reveal the presence of proteins similar to Ole e 3 in the pollen from non-related plant species, which may explain allergic cross-reactivity processes.
已从油橄榄（Olea europaea）花粉的盐提取物中分离出一种过敏原。通过质谱分析确定，该蛋白质由一条9.2 kDa的单多肽链组成。它既不含色氨酸残基也不含酪氨酸残基，并且具有酸性等电点。根据肽键区域的圆二色光谱分析估计，该蛋白质的二级结构由52%的α-螺旋、10%的β-链、29%的β-转角和9%的不规则构象组成。该蛋白质的N端被封闭。已从用CNBr处理天然过敏原产生的肽中获得氨基酸序列数据。由此阐明了36个氨基酸的部分序列。该蛋白质与芸苔属物种的花粉过敏原具有序列相似性，并含有一个Ca(2+)结合基序。分离出的蛋白质对油橄榄花粉过敏患者的血清表现出IgE结合活性。根据国际免疫学会命名委员会的建议，它被命名为Ole e 3。用针对Ole e 3的多克隆抗体进行的IgG ELISA抑制试验表明，在非相关植物物种的花粉中存在与Ole e 3相似的蛋白质，这可能解释了过敏交叉反应过程。
