Osterman J V, Eisemann C S
Infect Immun. 1978 Sep;21(3):866-73. doi: 10.1128/iai.21.3.866-873.1978.
Six proteins, previously established as major constituents of intact organisms, were identified in cell envelopes obtained from intrinsically radiolabeled Rickettsia prowazekii. Extrinsic radioiodination of intact organisms conducted at 0.5 micronM iodide indicated that protein 4 was the most peripheral, although protein 1 also had reactive groups exposed on the surface of the organisms. A 10-fold increase in iodide concentration resulted in labeling of protein 2, and at 50 micronM iodide, all six major proteins were radiolabeled. Similar selective labeling was not achieved with R. conorii. Analysis of both typhus and spotted fever group organisms radiolabeled with galactose suggested that carbohydrate was associated with proteins 1, 3, and 4. Typhus soluble antigen included all major proteins except protein 2, which remained attached to particulate rickettsiae after ether extraction. Protein 4 appeared to be prominent in the surface topography of R. prowazekii, was a component of soluble antigen and may have an important role in rickettsiae-host interactions.
在从内在放射性标记的普氏立克次体获得的细胞膜中，鉴定出六种先前被确定为完整生物体主要成分的蛋白质。在0.5微摩尔碘化物浓度下对完整生物体进行的外部放射性碘化表明，蛋白质4是最外周的，尽管蛋白质1在生物体表面也有暴露的反应基团。碘化物浓度增加10倍会导致蛋白质2被标记，在50微摩尔碘化物浓度下，所有六种主要蛋白质都被放射性标记。康氏立克次体未实现类似的选择性标记。对用半乳糖放射性标记的斑疹伤寒群和斑点热群生物体的分析表明，碳水化合物与蛋白质1、3和4相关。斑疹伤寒可溶性抗原包括除蛋白质2之外的所有主要蛋白质，蛋白质2在乙醚提取后仍附着于颗粒性立克次体。蛋白质4似乎在普氏立克次体的表面形貌中很突出，是可溶性抗原的一个成分，可能在立克次体与宿主的相互作用中起重要作用。
