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首页> 外文期刊>Infection and immunity >Coordinate synthesis and turnover of heat shock proteins in Borrelia burgdorferi: degradation of DnaK during recovery from heat shock.
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Coordinate synthesis and turnover of heat shock proteins in Borrelia burgdorferi: degradation of DnaK during recovery from heat shock.

机译：伯氏疏螺旋体中热激蛋白的协调合成和周转：从热激恢复过程中DnaK的降解。

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The synthesis and turnover of heat shock proteins (Hsps) by Borrelia burgdorferi, the Lyme disease spirochete, was investigated by radiolabeling of whole spirochetes and spheroplasts, comparison of one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and use of immunochemistry. The approximately 72-kDa DnaK homolog and three additional Hsps of 39, 27, and 21 kDa increased in amount by 3- to 15-fold between 2 and 6 h following temperature upshift from 28 to 39 degrees C. Temperature downshift experiments following the transfer of spirochetes from 40 to 28 degrees C showed that within 15 to 30 min, synthesis of most of the major Hsps returned to levels seen in spirochetes statically maintained at the lower temperature. Spheroplasts of B. burgdorferi produced by treatment with EDTA and lysozyme were radiolabeled, and specific Hsps were localized to either the cytoplasm or membrane fraction. Further analysis by two-dimensional electrophoresis demonstrated three constitutively expressed DnaK isoforms with pIs near 5.5. A pattern suggestive of DnaK degradation was observed following recovery from heat shock but not in spirochetes maintained entirely at a low temperature. Some of these putative degradation products were recognized by monoclonal antibodies directed against the B. burgdorferi DnaK protein. These data suggest that following a period of peak synthesis, DnaK is actively degraded as the spirochete reestablishes its metabolic thermometer. These findings provide a new interpretation of previous work suggesting that 10 to 15 B. burgdorferi polypeptides, including DnaK have a common epitope.
机译：通过对整个螺旋体和原生质球进行放射性标记，一维和二维十二烷基硫酸钠-聚丙烯酰胺凝胶电泳的比较以及免疫化学的使用，研究了伯氏疏螺旋体（莱姆病螺旋体）的热休克蛋白（Hsps）的合成和转换。 。在温度从28升高到39摄氏度后的2到6小时之间，大约72 kDa的DnaK同源物和另外的39、27和21 kDa的Hsps的量增加了3到15倍。转移后的温度降低的实验40至28摄氏度的螺旋桨显示，在15至30分钟内，大多数主要Hsps的合成恢复到静态保持在较低温度的螺旋桨中所见的水平。用EDTA和溶菌酶处理产生的B. burgdorferi原生质球被放射性标记，特定的Hsps定位于细胞质或膜部分。二维电泳的进一步分析表明，pI接近5.5的三种组成型表达的DnaK同工型。从热冲击中恢复后观察到暗示DnaK降解的模式，但在完全保持在低温下的螺旋体中未观察到。这些推定降解产物中的一些被针对伯氏疏螺旋体DnaK蛋白的单克隆抗体识别。这些数据表明，经过一段峰值合成后，随着螺旋体重新建立其代谢温度计，DnaK会被积极降解。这些发现为以前的工作提供了新的解释，表明包括DnaK在内的10至15个伯氏疏螺旋体多肽具有共同的表位。

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