Lundemose A G, Birkelund S, Fey S J, Larsen P M, Christiansen G
Institute of Medical Microbiology, University of Aarhus, Denmark.
Mol Microbiol. 1991 Jan;5(1):109-15. doi: 10.1111/j.1365-2958.1991.tb01831.x.
A 27kDa Chlamydia trachomatis L2 protein was characterized by the use of monoclonal antibodies and by two-dimensional gel electrophoresis. The protein was shown to be located in the membrane of reticulate bodies as well as elementary bodies. Its synthesis could be detected from 10 hours post-infection. Cloning and sequence analysis of the distal part of the gene revealed an open reading frame of 175 amino acids. Comparison of the deduced amino acid sequence with the NBRF data base revealed significant homology between the 27 kDa chlamydial membrane protein and the product of the macrophage infectivity potentiator (mip) gene of Legionella pneumophila.
通过使用单克隆抗体和二维凝胶电泳对沙眼衣原体L2的一种27kDa蛋白进行了特性分析。结果表明该蛋白位于网状体以及原体的膜中。在感染后10小时即可检测到其合成。对该基因远端部分进行克隆和序列分析,发现一个由175个氨基酸组成的开放阅读框。将推导的氨基酸序列与NBRF数据库进行比较,发现沙眼衣原体27kDa膜蛋白与嗜肺军团菌巨噬细胞感染增强因子(mip)基因的产物之间存在显著同源性。