Birkelund S, Larsen B, Holm A, Lundemose A G, Christiansen G
Institute of Medical Microbiology, University of Aarhus, Denmark.
Infect Immun. 1994 May;62(5):2051-7. doi: 10.1128/iai.62.5.2051-2057.1994.
A cytoplasmic 75-kDa immunogen from Chlamydia trachomatis serovar L2 has previously been characterized as being similar to the Escherichia coli heat shock protein DnaK. We have localized a linear epitope for one monoclonal antibody specific for C. trachomatis DnaK. By use of a recombinant DNA technique, the epitope was limited to 14 amino acids. With synthetic peptides, the epitope was further limited to eight amino acids. Six of these amino acids are conserved in bovine HSP70, which has a known three-dimensional structure. The amino acid sequence homologous to the epitope is located in a linear part of the HSP70 molecule known as connect II.
沙眼衣原体L2血清型的一种75 kDa细胞质免疫原先前已被鉴定为与大肠杆菌热休克蛋白DnaK相似。我们已经定位了一种针对沙眼衣原体DnaK的单克隆抗体的线性表位。通过使用重组DNA技术,该表位被限定为14个氨基酸。利用合成肽,该表位进一步被限定为8个氨基酸。其中6个氨基酸在具有已知三维结构的牛HSP70中是保守的。与该表位同源的氨基酸序列位于HSP70分子中称为连接II的线性部分。