Morrison R P, Su H, Lyng K, Yuan Y
Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840.
Infect Immun. 1990 Aug;58(8):2701-5. doi: 10.1128/iai.58.8.2701-2705.1990.
The Chlamydia trachomatis serovar A hyp operon was cloned, sequenced, and expressed in Escherichia coli. Two cotranscribed open reading frames, hypA and hypB, encoded polypeptides of 17 and 57 kilodaltons, respectively. The deduced amino acid sequences of serovar A HypA and HypB proteins were (respectively) 85 and 94% identical with HypA and HypB proteins of Chlamydia psittaci GPIC, and HypB was greater than 50% identical to 60-kilodalton stress response proteins from other procaryotes and eucaryotes. The sequence should be useful in defining the antigenic structure of the Chlamydia trachomatis HypB protein, a necessary step toward understanding the relationship between the immune response to this protein and the pathogenesis of human chlamydial diseases.
沙眼衣原体A血清型hup操纵子被克隆、测序并在大肠杆菌中表达。两个共转录的开放阅读框，hupA和hupB，分别编码17和57千道尔顿的多肽。血清型A HypA和HypB蛋白推导的氨基酸序列分别与鹦鹉热衣原体GPIC的HypA和HypB蛋白有85%和94%的同源性，并且HypB与来自其他原核生物和真核生物的60千道尔顿应激反应蛋白有超过50%的同源性。该序列对于确定沙眼衣原体HypB蛋白的抗原结构应是有用的，这是理解针对该蛋白的免疫反应与人类衣原体疾病发病机制之间关系的必要步骤。
