Zhang Y X, Shi Y, Zhou M, Petsko G A
Maxwell Finland Laboratory for Infectious Diseases, Boston City Hospital, Boston University School of Medicine, Massachusetts 02118.
J Bacteriol. 1994 Feb;176(4):1184-7. doi: 10.1128/jb.176.4.1184-1187.1994.
The gene encoding a 45-kDa protein (45K) of Chlamydia trachomatis serovar F was cloned, sequenced, and overexpressed in Escherichia coli. Alignment of the deduced peptide sequence with E. coli elongation factor Tu (EF-Tu) demonstrated 69% identity. The 45K was recognized by a Chlamydia genus-specific monoclonal antibody GP-45 and cross-reacted with a monospecific polyclonal antibody to E. coli EF-Tu. Purified recombinant 45K has the capability to bind GDP, and the binding was enhanced in the presence of E. coli elongation factor Ts (EF-Ts). The GDP binding was specifically inhibited by the monoclonal antibody GP-45. These data suggest that the 45K is a chlamydial EF-Tu, and it forms a functional complex with E. coli EF-Ts protein.
沙眼衣原体血清型F编码45 kDa蛋白(45K)的基因被克隆、测序,并在大肠杆菌中过表达。推导的肽序列与大肠杆菌延伸因子Tu(EF-Tu)比对显示有69%的同一性。45K被沙眼衣原体属特异性单克隆抗体GP-45识别,并与抗大肠杆菌EF-Tu的单特异性多克隆抗体发生交叉反应。纯化的重组45K具有结合GDP的能力,并且在大肠杆菌延伸因子Ts(EF-Ts)存在的情况下结合增强。GDP结合被单克隆抗体GP-45特异性抑制。这些数据表明45K是一种衣原体EF-Tu,并且它与大肠杆菌EF-Ts蛋白形成功能复合物。