Subcellular Localization and Cytotoxic Activity of the GroEL-Like Protein Isolated from Actinobacillus actinomycetemcomitans

F. Goulhen; A. Hafezi; V.-J. Uitto; D. Hinode; R. Nakamura; D. Grenier; D. Mayrand

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Subcellular Localization and Cytotoxic Activity of the GroEL-Like Protein Isolated from Actinobacillus actinomycetemcomitans

机译：从放线放线杆菌的GroEL样蛋白的亚细胞定位和细胞毒活性。

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The subcellular locations, ultrastructure, and cytotoxic activity of the GroEL-like protein from Actinobacillus actinomycetemcomitans were investigated. Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) clearly indicated that synthesis of the GroEL-like protein is substantially increased after a thermal shock. Analysis of the purified native GroEL-like protein by transmission electron microscopy revealed the typical 14-mer cylindrical molecule, which had a diameter of about 12 nm. A. actinomycetemcomitans cells grown at 35°C and heat shocked at 43°C were fractionated, and fractions were separated by SDS-PAGE and analyzed by Western immunoblotting using antibodies to GroEL- and DnaK-like proteins. The GroEL-like protein was found in both the soluble and membrane fractions, whereas the DnaK-like protein was mostly found in the cytoplasm. An increase in specific proteins, including the GroEL- and DnaK-like proteins, was found in heat-shocked cells. The subcellular localization of the GroEL-like protein was examined by immunoelectron microscopy of whole cells. More GroEL-like protein was detected in stressed cells than in unstressed cells, and most of it was found not directly associated with outer membranes but rather in extracellular material. The native GroEL-like protein was assessed for cytotoxic activities. The GroEL-like protein increased the proliferation of periodontal ligament epithelial cells at concentrations between 0.4 and 1.0 μg/ml. The number of cells in the culture decreased significantly at higher concentrations. A cell viability assay using HaCaT epithelial cells indicated that the GroEL-like protein was strongly toxic for the cells. These studies suggest the extracellular nature of the GroEL-like protein and its putative role in disease initiation.

机译：研究了放线放线杆菌放线杆菌GroEL样蛋白的亚细胞定位，超微结构和细胞毒活性。二维十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）清楚地表明，热冲击后，GroEL样蛋白的合成大大增加。通过透射电子显微镜对纯化的天然GroEL样蛋白的分析显示出典型的14聚体圆柱分子，其直径约为12nm。 A。将在35°C生长并在43°C热激的放线放线杆菌细胞进行分级，并通过SDS-PAGE分离级分，并使用针对GroEL和DnaK样蛋白的抗体通过Western免疫印迹进行分析。在可溶性和膜级分中均发现了GroEL样蛋白，而在细胞质中大多发现了DnaK样蛋白。在热激细胞中发现特定蛋白质的增加，包括GroEL和DnaK样蛋白质。 GroEL样蛋白的亚细胞定位通过全细胞的免疫电子显微镜检查。在受压细胞中检测到的GroEL样蛋白多于未受压细胞，并且发现大多数与外膜不直接相关，而与细胞外物质相关。评价天然的GroEL样蛋白的细胞毒性活性。 GroEL样蛋白在0.4和1.0μg/ ml之间的浓度下增加了牙周膜上皮细胞的增殖。在较高浓度下，培养物中的细胞数量显着减少。使用HaCaT上皮细胞的细胞活力分析表明，GroEL样蛋白对细胞具有强烈毒性。这些研究表明，GroEL样蛋白的细胞外性质及其在疾病引发中的假定作用。 展开▼

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《Infection and immunity》 |1998年第11期|共7页

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F. Goulhen; A. Hafezi; V.-J. Uitto; D. Hinode; R. Nakamura; D. Grenier; D. Mayrand;
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中图分类医学免疫学;

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机译：分离的蛋白质，基本上纯的或重组的分离的trt蛋白，基本上纯的或重组的分离的trt蛋白，基本上纯的或重组的分离的trt蛋白或其变体或片段，多核苷酸，合成的，基本上纯的或重组的分离的核酸的制备编码trt蛋白的酸，表达载体，转染的细胞，非人类动物或其后代，转基因非人类动物，抗体或其结合片段，抗体，在免疫反应条件下对trt蛋白或其免疫原具有特异性片段，确定化合物或处理是否是trt活性或表达的调节剂，确定测试化合物是否是trt活性的调节剂，制备重组端粒酶以检测样品中trt基因产物的过程，检测包含人细胞的生物样品中d和至少一种端粒酶阳性人细胞的存在，以进行诊断

4. THE CAGE GENE OF ACTINOBACILLUS ACTINOMYCETEMCOMITANS, THE PROTEIN IT ENCODES AND USES THEREOF [P] . 外国专利： WO03002745A2 . 2003-01-09

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5. THE CAGE GENE OF ACTINOBACILLUS ACTINOMYCETEMCOMITANS, THE PROTEIN IT ENCODES AND USES THEREOF [P] . 外国专利： WO03002745A3 . 2003-12-11

机译：猕猴桃放线菌的笼型基因，其编码的蛋白质及其用途

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Subcellular Localization and Cytotoxic Activity of the GroEL-Like Protein Isolated from Actinobacillus actinomycetemcomitans

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