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肺炎支原体通过分子模拟来逃避诱导黏附抑制抗体。

Molecular mimicry by Mycoplasma pneumoniae to evade the induction of adherence inhibiting antibodies.

作者信息

Jacobs E, Bartl A, Oberle K, Schiltz E

机构信息

Institute for Medical Microbiology and Hygiene, University of Freiburg, Germany.

出版信息

J Med Microbiol. 1995 Dec;43(6):422-9. doi: 10.1099/00222615-43-6-422.

DOI:10.1099/00222615-43-6-422
PMID:7473675
Abstract

Specific regions of adherence binding sites and epitopes of the P1 adhesin of Mycoplasma pneumoniae were synthesised as octapeptides and used as targets in a modified enzyme-linked immunosorbent assay. Acute phase and convalescent sera from 10 patients with M. pneumoniae infection were tested for antibody reactivity to these octapeptides. In convalescent sera, antibody activities were directed against octapeptides of the epitope regions, whereas no antibody activity was found in acute or convalescent sera to octapeptides of adherence-mediating binding sites could be explained partially from the results of cross-reactivity experiments with adherence-inhibiting anti-P1 adhesin monoclonal antibodies (MAbs). Two of these MAbs showed cross-reactions with intracellular antigens of eukaryotic cell lines in immunofluorescence microscopy experiments. The cross-reacting antigens were isolated and characterised as glyceraldehyde-3-phosphate dehydrogenase and 2-phospho-D-glycerate hydrolyase. Antigenic mimicry of eukaryotic structures by functional sites of the P1 adhesin of M. pneumoniae may influence the pathogenesis of M. pneumoniae infection.

摘要

肺炎支原体P1黏附素的黏附结合位点和表位的特定区域被合成为八肽,并用作改良酶联免疫吸附测定中的靶标。对10例肺炎支原体感染患者的急性期和恢复期血清进行检测,以确定其对这些八肽的抗体反应性。在恢复期血清中,抗体活性针对表位区域的八肽,而在急性期或恢复期血清中未发现针对黏附介导结合位点八肽的抗体活性,这可以部分地从与黏附抑制性抗P1黏附素单克隆抗体(MAb)的交叉反应实验结果中得到解释。其中两种单克隆抗体在免疫荧光显微镜实验中与真核细胞系的细胞内抗原有交叉反应。对交叉反应抗原进行了分离和鉴定,结果表明它们是甘油醛-3-磷酸脱氢酶和2-磷酸-D-甘油酸水解酶。肺炎支原体P1黏附素的功能位点对真核结构的抗原模拟可能会影响肺炎支原体感染的发病机制。

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