THE IMMUNODOMINANT 90-KILODALTON PROTEIN IS LOCALIZED ON THE TERMINAL TIP STRUCTURE OF MYCOPLASMA-PNEUMONIAE
THE IMMUNODOMINANT 90-KILODALTON PROTEIN IS LOCALIZED ON THE TERMINAL TIP STRUCTURE OF MYCOPLASMA-PNEUMONIAE
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DOI：
10.1128/iai.61.4.1523-1530.1993
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发表时间：
1993-04-01
影响因子：
3.1
通讯作者：
BARILE, MF
中科院分区：
文献类型：
--
作者：
FRANZOSO, G;HU, PC;BARILE, MF
对实验感染的黑猩猩恢复期血清或肺炎支原体90和40 kDa蛋白的单抗的免疫印迹分析表明，这两种蛋白都存在于细胞吸附致病株PI-1428、M129和FH中，而在不吸附细胞的非致病株M129-B176中不存在。恢复期黑猩猩血清与强毒株PI-1428的吸附去除了反应性，而与强毒株M129-B176的吸附不能去除对这两种蛋白的反应性。通过蛋白水解法和特异性单抗，我们证明了90 kDa和40 kDa的蛋白被暴露在表面。使用特定单抗的免疫电子显微镜显示，90 kDa的蛋白定位在末端附着器上。然而，针对40 kDa蛋白的单抗未能显示类似的定位。然而，这些数据综合起来，表明免疫优势的90-和40-kDa蛋白表面暴露，定位于末端装置，并可能参与附着机制。
Immunoblot analysis of convalescent-phase sera of experimentally infected chimpanzees or monoclonal antibodies (MAbs) specific to the 90- and 40-kDa proteins of Mycoplasma pneumoniae indicated that both proteins were present in cytadsorbing, pathogenic strains PI-1428, M129, and FH but absent in noncytadsorbing, nonpathogenic strain M129-B176. Adsorption of convalescent-phase chimpanzee sera with virulent strain PI-1428 removed reactivity, whereas adsorption with avirulent strain M129-B176 did not remove reactivity to these two proteins. By using proteolysis and specific MAbs, we demonstrated that the 90- and 40-kDa proteins were surface exposed. Immunoelectron microscopy employing specific MAbs showed that the 90-kDa protein is localized on the terminal tip attachment apparatus. However, the MAb specific for the 40-kDa protein failed to indicate a similar localization. Nevertheless, these data, taken together, indicate that the immunodominant 90- and 40-kDa proteins are surface exposed, are localized on the terminal tip apparatus, and might be involved in the attachment mechanism.