Kaul R, Roy K L, Wenman W M
Department of Pediatrics, University of Alberta, Edmonton, Canada.
J Bacteriol. 1987 Nov;169(11):5152-6. doi: 10.1128/jb.169.11.5152-5156.1987.
The gene encoding an 18,000-dalton eucaryotic cell-binding protein of Chlamydia trachomatis serovar L2 was cloned into Escherichia coli, and the nucleotide sequence of a 1,658-base-pair PstI restriction endonuclease fragment encoding this protein was determined. The recombinant chlamydial gene consists of a 486-base-pair open reading frame encoding a polypeptide of molecular weight 18,314. The resultant polypeptide, comprising 162 amino acids, possesses a highly charged carboxy-terminal end. The expression of this recombinant protein is under the control of a vector promoter. The recombinant 18,000-dalton protein possessed the same eucaryotic cell-binding characteristics as did the native chlamydial 18,000-dalton protein when electrophoresed and transferred to nitrocellulose. Polyclonal antibodies to the recombinant protein exhibited neutralizing activity.
沙眼衣原体L2血清型编码18000道尔顿真核细胞结合蛋白的基因被克隆到大肠杆菌中，并测定了编码该蛋白的1658个碱基对的PstI限制性内切酶片段的核苷酸序列。重组衣原体基因由一个486个碱基对的开放阅读框组成，编码分子量为18314的多肽。所得多肽由162个氨基酸组成，具有高度带电的羧基末端。该重组蛋白的表达受载体启动子的控制。当进行电泳并转移到硝酸纤维素膜上时，重组的18000道尔顿蛋白具有与天然衣原体18000道尔顿蛋白相同的真核细胞结合特性。针对该重组蛋白的多克隆抗体表现出中和活性。
