Fan J Y, Davidson E A
Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, Washington, District of Columbia, USA.
Am J Trop Med Hyg. 1996 Nov;55(5):570-6. doi: 10.4269/ajtmh.1996.55.570.
We have isolated a 70-kD heat-shock protein (hsp-70) cDNA from Plasmodium berghei. A cDNA clone encoding the P. berghei hsp-70 was isolated and sequenced, demonstrating that it is highly homologous with other Plasmodium hsp-70s. One of the common features is a series of GGMP amino acid repeats at the carboxy terminus; there is also a long, AT-rich 5' untranslated region, a hallmark of other malarial RNAs. Hydropathy and antigenicity analyses suggest the presence of two hydrophilic domains. Recombinant peptides comprising different fragments of hsp-70 were expressed in Escherichia coli and assessed for antigenicity with antiserum from mice immunized with sonicated extracts of P. berghei. Antigenic sites map to regions that include the two hydrophilic domains.
我们从伯氏疟原虫中分离出了一个70-kD热休克蛋白（hsp-70）的cDNA。一个编码伯氏疟原虫hsp-70的cDNA克隆被分离并测序，结果表明它与其他疟原虫的hsp-70高度同源。一个共同特征是在羧基末端有一系列GGMP氨基酸重复序列；此外还有一个长的、富含AT的5'非翻译区，这是其他疟原虫RNA的一个标志。亲水性和抗原性分析表明存在两个亲水区。包含hsp-70不同片段的重组肽在大肠杆菌中表达，并用来自用伯氏疟原虫超声提取物免疫的小鼠的抗血清评估其抗原性。抗原位点定位于包括两个亲水区的区域。
