Identification and characterization of a uroepithelial cell adhesin from a uropathogenic isolate of Proteus mirabilis
Identification and characterization of a uroepithelial cell adhesin from a uropathogenic isolate of Proteus mirabilis
复制标题
DOI：
10.1128/iai.54.1.43-49.1986
复制
发表时间：
1986-10
影响因子：
3.1
通讯作者：
S. K. Wray;S. Hull;R. Cook;J. Barrish;R. Hull
中科院分区：
文献类型：
--
作者：
S. K. Wray;S. Hull;R. Cook;J. Barrish;R. Hull
奇异变形杆菌是康复医院和尿路结构异常患者尿路感染的常见原因。对尿上皮组织的粘附可能是这些感染中重要的毒力决定因素，因为大多数变形杆菌菌株粘附于脱落的尿上皮细胞。为了确定导致这种现象的粘附因素，我们从 35SO4 放射性标记的细菌中剪下外膜材料，并使其与尿上皮细胞结合。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳后，主要粘附成分是表观分子量为17,500的蛋白质，暂时命名为尿路上皮细胞粘附素。通过热休克和琼脂糖 CL-4B 上的凝胶过滤纯化该粘附素。纯化后，通过电子显微镜观察粘附素组装成长而柔韧的棒。该亚基的N端氨基酸序列与大肠杆菌K99菌毛的N端氨基酸序列具有有限的同源性。
Proteus mirabilis is a frequent cause of urinary tract infections in rehabilitation hospitals and among persons with structural abnormalities of the urinary tract. Adherence to uroepithelial tissues may be an important virulence determinant in these infections because most Proteus strains adhere to desquamated uroepithelial cells. To identify the adherence factor responsible for this phenomenon, we sheared outer membrane material from 35SO4-radiolabeled bacteria and allowed it to bind to uroepithelial cells. Following sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the major adherence element was a protein with an apparent molecular weight of 17,500 and was provisionally designated as the uroepithelial cell adhesin. This adhesin was purified by heat shock and gel filtration on Sepharose CL-4B. After purification, the adhesin was seen assembled as long, flexible rods by electron microscopy. The N-terminal amino acid sequence of the subunit had limited homology with that of the K99 fimbriae of Escherichia coli.