MOLECULAR CHAPERONES

B.百日咳，产生的主要分子伴侣， 这种生物的研究。 这种蛋白质具有十四聚体 GroEL蛋白家族的典型结构。 进行研究 研究cpn 60的结构和功能关系， 更好地理解这种蛋白质在蛋白质折叠中的作用。 一种与两种B结合的IgG单克隆抗体（mAb 54 G8）。百日咳 cpn 60和大肠杆菌cpn 60（GroEL）被发现可以消除这种能力 的cpn 10抑制ATP酶活性cpn 60，而不管的来源。 这种蛋白质。 通过电子显微镜显示MAb 54 G8结合至 十四聚体CPN 60分子。 电子计算机图像处理 拍摄cpn 60-Ab的显微照片。 cpn 60-Ab复合物的抑制 从各个侧视图中可以看出， 从CPN 60分子的任一个六面的角。 不再 两种以上的抗体似乎结合在CPN 60的每一端。 的平均值 cpn 60分子仅与Fab相互作用的电子显微照片 当与Fab相互作用时，抗体的一部分显示出受到干扰 片段 我们的数据表明mAb 54 G8在cpn 60末端的结合 部分影响CPN 60与CPN 10有效相互作用的能力。

The cpn60 protein of B. pertussis, the major molecular chaperone produced by this organism was studied. This protein has the tetradecameric structure typical of the GroEL family of proteins. Studies were conducted to examine the structure/function relationships of cpn60 in the hope of better understanding the role that this protein plays in protein folding. An IgG monoclonal antibody (mAb 54G8) which binds to both B. pertussis cpn60 and Escherichia coli cpn60 (GroEL) was found to abolish the ability of cpn10 to inhibit the ATPase activity cpn60 regardless of the source of this protein. MAb 54G8 was shown by electron microscopy to bind to ends of the tetradecameric cpn60 molecules. Computer image processing of electron micrographs of the cpn60-Ab was performed. Averages of cpn60-Ab complex from individual side views shown centers of mass attached to and extending from the corners of either hepameric face of the cpn60 molecule. No more than two antibodies appear to bind at each end of cpn60. Averages of electron micrographs of cpn60 molecules interacting with only the Fab portion of the antibody show to be perturbed when interacting with Fab fragments. Our data suggest that binding of mAb 54G8 at the end of cpn60 partially affects the ability of cpn60 productively interact with cpn10.