Namba M, Kurose M, Torigoe K, Hino K, Taniguchi Y, Fukuda S, Usui M, Kurimoto M
Fujisaki Institute, Hayashibara Biochemical Laboratories Inc., Okayama, Japan.
FEBS Lett. 1994 Oct 17;353(2):124-8. doi: 10.1016/0014-5793(94)01022-6.
Cloning of a cDNA from Cry j II, the second major allergen from Japanese cedar (Cryptomeria japonica) pollen, is described. An isolated Cry j II cDNA contained an open reading frame coding for 514 amino acid residues. The mature Cry j II protein consisted of 388 amino acid residues (R46-S433). According to a homology analysis, no amino acid sequence homology was observed between Cry j II and Cry j I, another major allergen. But Cry j II showed homology with polygalacturonase (PG) derived from tomato (40% identity) at the amino acid level. The sequence information can potentially be used to devise an effective course of immunotherapy for Japanese cedar pollinosis.
本文描述了从日本柳杉(Cryptomeria japonica)花粉的第二大主要过敏原Cry j II中克隆cDNA的过程。分离得到的Cry j II cDNA包含一个编码514个氨基酸残基的开放阅读框。成熟的Cry j II蛋白由388个氨基酸残基组成(R46 - S433)。根据同源性分析,未观察到Cry j II与另一种主要过敏原Cry j I之间的氨基酸序列同源性。但Cry j II在氨基酸水平上与源自番茄的多聚半乳糖醛酸酶(PG)具有同源性(一致性为40%)。该序列信息有可能用于设计针对日本柳杉花粉症的有效免疫治疗方案。