Bölin I, Forsberg A, Norlander L, Skurnik M, Wolf-Watz H
National Defence Research Institute, Umea, Sweden.
Infect Immun. 1988 Feb;56(2):343-8. doi: 10.1128/iai.56.2.343-348.1988.
The structural genes of the outer membrane polypeptides of Yersinia spp. (YOPs) and the V antigen of plasmid pIB1 of Yersinia pseudotuberculosis were recently cloned and mapped (A. Forsberg, I. Bölin, L. Norlander, and H. Wolf-Watz, Microb. Pathogen. 2:123-137, 1987). The corresponding genes were localized on pYV019 and pYV8081 of Yersinia pestis and Yersinia enterocolitica, respectively. No obvious differences were observed on comparison of pIB1 and pYV019, whereas pYV8081 showed intragenic as well as extragenic changes. However, one region of plasmid pYV8081, which coded for the V antigen, YOP3, and YOP4a, was essentially conserved among the three plasmids. Since this region is connected with the Ca2+ region, we suggest that the conserved region of the virulence plasmids of Yersinia spp. be extended to include both of these regions. Low amounts of the YOPs were detected in the membrane fraction at 37 degrees C in the presence of 2.5 mM calcium. Only minor differences were noticed when the individual YOPs of Y. pestis and Y. pseudotuberculosis were compared. Several differences were observed when the YOPs of Y. enterocolitica were included for comparison. All Y. enterocolitica proteins, except YOP1, YOP4b, and the V antigen, exhibited changes in their characteristic molecular sizes. Although these differences were within a range of +/- 2 kilodaltons, the isoelectric point was retained for each protein type.
耶尔森氏菌属外膜多肽(YOPs)的结构基因以及假结核耶尔森氏菌质粒pIB1的V抗原最近已被克隆并定位(A. 福斯伯格、I. 博林、L. 诺兰德和H. 沃尔夫 - 瓦茨,《微生物病原体》2:123 - 137,1987年)。相应基因分别定位于鼠疫耶尔森氏菌的pYV019和小肠结肠炎耶尔森氏菌的pYV8081上。比较pIB1和pYV019时未观察到明显差异,而pYV8081显示出基因内以及基因外的变化。然而,质粒pYV8081编码V抗原、YOP3和YOP4a的一个区域在这三种质粒中基本保守。由于该区域与Ca2 +区域相连,我们认为耶尔森氏菌属毒力质粒的保守区域应扩展至包括这两个区域。在2.5 mM钙存在的情况下,于37℃在膜组分中检测到少量的YOPs。比较鼠疫耶尔森氏菌和假结核耶尔森氏菌的各个YOPs时仅注意到微小差异。当纳入小肠结肠炎耶尔森氏菌的YOPs进行比较时观察到了一些差异。除YOP1、YOP4b和V抗原外,所有小肠结肠炎耶尔森氏菌蛋白在其特征性分子大小上均表现出变化。尽管这些差异在±2千道尔顿范围内,但每种蛋白类型的等电点保持不变。