IDENTIFICATION AND PARTIAL CHARACTERIZATION OF RICKETTSIA-TSUTSUGAMUSHI MAJOR PROTEIN IMMUNOGENS
IDENTIFICATION AND PARTIAL CHARACTERIZATION OF RICKETTSIA-TSUTSUGAMUSHI MAJOR PROTEIN IMMUNOGENS
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DOI：
10.1128/iai.50.3.603-609.1985
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发表时间：
1985-01-01
影响因子：
3.1
通讯作者：
HANSON, B
中科院分区：
文献类型：
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作者：
HANSON, B
迄今为止，所研究的恙虫病立克次体菌株具有三种或四种数量上占优势的蛋白质，它们显然是表面蛋白，大小在50至63千道尔顿之间。这些多肽也是用高免疫兔血清沉淀的立克次体蛋白的聚丙烯酰胺凝胶电泳检测到的主要免疫原。来自不同立克次体菌株的主要蛋白质共享一些表位，如在免疫沉淀试验中兔血清缺乏菌株特异性所证明的。然而，用有限数量的单克隆抗体进行的类似实验表明，菌株特异性决定簇也与至少58/60千道尔顿多肽相关。立克次体表面缺乏菌株特异性表位，这表明我们无法通过免疫铁蛋白标记检测异源抗血清与立克次体表面的结合。由于Karp和Gilliam菌株的三种主要蛋白质在未提取的生物体中可接近抗体，因此这三种多肽的外部暴露表位可能是菌株特异性的，并且它们的共同决定簇通常埋藏在膜中或以其他方式不可接近。尝试吸收出特异性抗体与完整的立克次体给出了模棱两可的结果，然而，当免疫复合物形成前立克次体提取进行了检查，电泳，抗体似乎已经结合菌株特异性与至少60千道尔顿的蛋白质。
Strains of Rickettsia tsutsugamushi so far examined have either three or four quantitatively predominant proteins, which apparently are surface proteins and which range in size between 50 and 63 kilodaltons. These polypeptides also were the major immunogens detected by polyacrylamide gel electrophoresis of extracted rickettsial proteins which had been precipitated by hyperimmune rabbit sera. The major proteins from different rickettsial strains share some epitopes, as evidenced by the lack of strain specificity of the rabbit sera in the immunoprecipitation tests. However, similar experiments with a limited number of monoclonal antibodies showed that strain-specific determinants also are associated with at least the 58/60-kilodalton polypeptide. A lack of strain-specific epitopes on the rickettsial surface was indicated by our inability to detect binding of heterologous antisera to the rickettsial surface by immunoferritin labeling. Because the three major proteins of the Karp and Gilliam strains are accessible to antibody in unextracted organisms, it is possible that the exteriorly exposed epitopes of these three polypeptides are strain specific and that their common determinants are normally buried in the membrane or otherwise inaccessible. Attempts to absorb out specific antibody with intact rickettsiae gave equivocal results; however, when immune complexes formed before rickettsial extraction were examined by electrophoresis, antibody appeared to have bound strain specifically with at least the 60-kilodalton protein.