Valenta R, Duchêne M, Pettenburger K, Sillaber C, Valent P, Bettelheim P, Breitenbach M, Rumpold H, Kraft D, Scheiner O
Institute of General and Experimental Pathology, University of Vienna, Austria.
Science. 1991 Aug 2;253(5019):557-60. doi: 10.1126/science.1857985.
A complementary DNA encoding a pollen allergen from white birch (Betula verrucosa) that was isolated from a pollen complementary DNA library with serum immunoglobulin E from a birch pollen-allergic individual revealed significant sequence homology to profilins. The recombinant protein showed high affinity to poly-L-proline. Immunoglobulin E antibodies from allergic individuals bound to natural and recombinant birch profilin and also to human profilin. In addition, birch and human profilin induced histamine release from blood basophils of profilin-allergic individuals, but not of individuals sensitized to other plant allergens. The structural similarity of conserved proteins might therefore be responsible for maintaining immunoglobulin E antibody titers in type I allergy.
从白桦花粉互补DNA文库中分离出一种编码白桦（疣枝桦）花粉变应原的互补DNA，该文库使用来自一名桦树花粉过敏个体的血清免疫球蛋白E，结果显示与肌动蛋白结合蛋白具有显著的序列同源性。重组蛋白对聚-L-脯氨酸表现出高亲和力。过敏个体的免疫球蛋白E抗体与天然和重组白桦肌动蛋白结合蛋白以及人类肌动蛋白结合蛋白均发生结合。此外，白桦和人类肌动蛋白结合蛋白可诱导肌动蛋白结合蛋白过敏个体的血液嗜碱性粒细胞释放组胺，但对其他植物变应原致敏的个体则无此作用。因此，保守蛋白的结构相似性可能是维持I型过敏中免疫球蛋白E抗体滴度的原因。
