Arruda L K, Platts-Mills T A, Fox J W, Chapman M D
Department of Internal Medicine, University of Virginia, Charlottesville 22908.
J Exp Med. 1990 Nov 1;172(5):1529-32. doi: 10.1084/jem.172.5.1529.
A major 18-kD IgE-binding protein from Aspergillus fumigatus (Asp fI) has been purified. Partial amino acid sequencing of Asp f I showed extensive sequence homology (95%) between Asp fI and a cytotoxin (mitogillin) produced by A. restrictus. Crossinhibition radioimmunoassay using murine monoclonal antibody and human IgG and IgE antibodies showed that Asp fI and mitogillin were antigenically indistinguishable. Furthermore, both proteins inhibited protein synthesis in vitro by greater than 90%. Asp fI was expressed in A. fumigatus but not in seven other Aspergillus species. The results suggest that Asp fI could play a dual role in the pathogenesis of A. fumigatus-related diseases by promoting colonization through cytotoxic activity and by causing inflammatory reactions involving IgE antibodies.
来自烟曲霉的一种主要的18-kD IgE结合蛋白(Asp fI)已被纯化。Asp fI的部分氨基酸序列分析表明,Asp fI与局限曲霉产生的一种细胞毒素(丝裂毒素)之间存在广泛的序列同源性(95%)。使用鼠单克隆抗体以及人IgG和IgE抗体进行的交叉抑制放射免疫测定表明,Asp fI和丝裂毒素在抗原性上无法区分。此外,这两种蛋白在体外均能抑制超过90%的蛋白质合成。Asp fI在烟曲霉中表达,但在其他七种曲霉属物种中不表达。结果表明,Asp fI可能在烟曲霉相关疾病的发病机制中发挥双重作用,即通过细胞毒性活性促进定植,并通过引发涉及IgE抗体的炎症反应。