MOLECULAR CHAPERONES

分子伴侣

• 批准号: 3770287
• 负责人: D L BURNS
• 金额: --
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3770287
• 关键词: Bordetella pertussis; antigen antibody reaction; binding proteins; electron microscopy; image processing; immunoglobulin structure; molecular chaperones; monoclonal antibody; protein folding; protein structure function

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.

百日咳杆菌产生的主要分子伴侣蛋白cpn60 对该菌进行了研究。这种蛋白质具有十四聚体 GroEL蛋白质家族的典型结构。进行了研究 研究cpn60的结构/功能关系，以期 更好地了解这种蛋白质在蛋白质折叠中所起的作用。 一种与百日咳杆菌结合的免疫球蛋白单抗(MAb54G8) Cpn60和大肠杆菌cpn60(GroEL)被发现可以消除这种能力 Cpn10抑制ATPase活性cpn60，而不考虑其来源 这种蛋白质。 电子显微镜观察表明，单抗54G8可结合到病毒的末端 十四聚体cpn60分子。电子的计算机图像处理 对cpn60-Ab进行了显微照相。Cpn60-抗体复合体的平均值 从单独的侧视图可以看出重心附着并延伸 从cpn60分子的两个七分面的角。不再 在cpn60的两端似乎各有两个抗体结合。的平均值 Cpn60分子只与Fab相互作用的电子显微照片 部分抗体在与Fab相互作用时表现出扰动 碎片。我们的数据表明，单抗54G8在cpn60末端的结合 部分影响cpn60与cpn10的有效相互作用能力。