Yamamoto T, Miura H, Ohsumi K, Yamaguchi H, Taguchi H, Ogata S
Department of Microbiology, Kyorin University School of Medicine, Tokyo.
Res Microbiol. 1993 Nov-Dec;144(9):691-701. doi: 10.1016/0923-2508(93)90033-x.
Yersinia enterocolitica, a highly antigenic 60-kDa protein, designated cross-reacting protein antigen (CRPA), is a member of the chaperonin-60 family of molecular chaperones. The gene encoding CRPA was cloned, expressed and sequenced. A partial library from Y. enterocolitica 0:3 genomic DNA was constructed in vector pUC19 and was screened by the immunoreactivity to monoclonal antibody 1A4, which has specificity for a species-specific epitope on the CRPA molecule. The crpA gene region consists of a putative two-cistron operon encoding proteins of 549 and 97 amino acids. The operon structure was led by a consensus heat-shock promoter sequence. Homology searches using the derived amino acid sequence have revealed that CRPA is 88.2% identical to GroEL of Escherichia coli. CRPB, another protein encoded by the operon, shows extensive sequence homology, 91.8% identical to GroES of E. coli which is a member of chaperonin-10.
小肠结肠炎耶尔森菌的一种高度抗原性的60 kDa蛋白，称为交叉反应蛋白抗原（CRPA），是分子伴侣伴侣蛋白60家族的成员。编码CRPA的基因被克隆、表达并测序。构建了来自小肠结肠炎耶尔森菌0:3基因组DNA的部分文库，该文库在载体pUC19中构建，并通过对单克隆抗体1A4的免疫反应性进行筛选，该抗体对CRPA分子上的物种特异性表位具有特异性。crpA基因区域由一个推测的双顺反子操纵子组成，该操纵子编码549和97个氨基酸的蛋白质。该操纵子结构由一个共有热休克启动子序列引导。使用推导的氨基酸序列进行同源性搜索发现，CRPA与大肠杆菌的GroEL有88.2%的同一性。该操纵子编码的另一种蛋白质CRPB显示出广泛的序列同源性，与作为伴侣蛋白10成员的大肠杆菌GroES有91.8%的同一性。
