Boisset N, Penczek P, Taveau J C, Lamy J, Frank J, Lamy J
URA 1334 CNRS, Tours, France.
J Struct Biol. 1995 Jul-Aug;115(1):16-29. doi: 10.1006/jsbi.1995.1025.
An immunocomplex formed by the 4 x 6 meric hemocyanin of the scorpion Androctonus australis with the monoclonal antibody L104 was studied by cryoelectron microscopy and subjected to three-dimensional (3D) reconstruction. The reconstructed particle reflects the structure of the immunocomplex in its hydrated state and is devoid of the flattening that was previously observed with a negatively stained preparation. A 3D fitting of the X-ray data of the Panulirus interruptus hemocyanin and of the Fab R19.9 to the reconstruction volume allowed the first quantitative measurement of the structural parameters of the antigen, and the localization of the epitope at the surface of subunit Aa6. The independent alignment of the Fabs and the hexamers provides a direct verification for the accuracy of the fit and allows the building of the most detailed model of a cheliceratan 4 x 6meric complex and its attached monoclonal antibodies.
利用冷冻电子显微镜对由澳大利亚杀人蝎的4×6聚体血蓝蛋白与单克隆抗体L104形成的免疫复合物进行了研究,并进行了三维(3D)重建。重建后的颗粒反映了免疫复合物在水合状态下的结构,且没有出现之前在负染制剂中观察到的扁平化现象。将中断岩龙虾血蓝蛋白和Fab R19.9的X射线数据与重建体积进行3D拟合,首次对抗原的结构参数进行了定量测量,并确定了表位在亚基Aa6表面的位置。Fab片段和六聚体的独立比对直接验证了拟合的准确性,并有助于构建最详细的螯肢动物4×6聚体复合物及其附着单克隆抗体的模型。