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对脑膜炎奈瑟菌P1.7 PorA蛋白具有特异性的人源和鼠源单克隆IgG的比较。

A comparison of human and murine monoclonal IgGs specific for the P1.7 PorA protein of Neisseria meningitidis.

作者信息

Delvig A, Jahn S, Kusecek B, Heckels J E, Rosenqvist E, Høiby E A, Michaelsen T E, Achtman M

机构信息

Max Planck Institut für molekulare Genetik, Berlin, Germany.

出版信息

Mol Immunol. 1994 Nov;31(16):1257-67. doi: 10.1016/0161-5890(94)90076-0.

Abstract

Monoclonal human IgG SS269 reacts with Neisseria meningitidis expressing the P1.7 PorA protein and with linear peptides containing NGGAS, which accounts for the P1.7 specificity. Murine monoclonal antibody to P1.7 reacts with peptides containing the overlapping epitope, ASGQ. The human and murine antibodies have similar affinities. The low avidity human antibody is very inefficient at stimulating complement-mediated bactericidal killing while the high avidity murine antibody efficiently kills bacteria. However, efficient opsonophagocytosis was mediated even at low concentrations of the human antibody and in the absence of complement, suggesting that low avidity antibodies might be protective against disease.

摘要

单克隆人IgG SS269与表达P1.7 PorA蛋白的脑膜炎奈瑟菌以及含有NGGAS的线性肽发生反应,这解释了P1.7的特异性。针对P1.7的鼠单克隆抗体与含有重叠表位ASGQ的肽发生反应。人和鼠抗体具有相似的亲和力。低亲和力的人抗体在刺激补体介导的杀菌杀伤方面效率非常低,而高亲和力的鼠抗体能有效杀死细菌。然而,即使在低浓度的人抗体且无补体的情况下,也能介导有效的调理吞噬作用,这表明低亲和力抗体可能对疾病具有保护作用。

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