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Binding sites of attachment-inhibiting monoclonal antibodies and antibodies from patients on peptide fragments of the Mycoplasma pneumoniae adhesin.

机译:抑制附着的单克隆抗体和患者抗体在肺炎支原体粘附素肽片段上的结合位点。

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The adherence protein (P1 protein) of Mycoplasma pneumoniae was purified by electroelution and cleaved with cyanogen bromide. The resulting peptides were separated by two-dimensional electrophoresis. Spots reacting in Western immunoblots with two attachment-inhibiting monoclonal antibodies were isolated, and the amino-terminal ends of these peptides were microsequenced. The two monoclonal antibodies had different binding sites. One was associated with the amino-terminal region of the whole P1 protein beginning at amino acid position 237, and the other was associated with amino acid position 702, which was localized approximately in the middle of the P1 amino acid sequence. Serum samples from three M. pneumoniae-infected patients were tested by Western blotting against the cyanogen bromide peptide pattern. All three serum samples reacted with peptide fragments beginning at amino acid position 702, but the serum of only one patient also had antibodies against the oligopeptides beginning at amino acid position 237. These results indicate that the corresponding epitopes of the P1 protein are also immunogenic if they are presented at the surface of the infecting organism.
机译:通过电洗脱纯化肺炎支原体的粘附蛋白(P1蛋白),并用溴化氰裂解。通过二维电泳分离得到的肽。分离了在Western免疫印迹中与两种抑制附着的单克隆抗体反应的斑点,并对这些肽的氨基末端进行了微测序。两种单克隆抗体具有不同的结合位点。一个与整个P1蛋白的氨基末端区域(从氨基酸位置237开始)相关,另一个与氨基酸位置702(位于大约P1氨基酸序列的中间)相关。通过蛋白质印迹针对溴化氰肽图谱测试了三名肺炎支原体感染患者的血清样品。所有三个血清样品均与始于氨基酸位置702的肽片段发生反应,但只有一名患者的血清也具有针对始于氨基酸位置237的寡肽的抗体。这些结果表明,P1蛋白的相应表位也具有免疫原性它们存在于感染生物的表面。

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