Electron and X-ray diffraction studies of influenza neuraminidase complexed with monoclonal antibodies.
Electron and X-ray diffraction studies of influenza neuraminidase complexed with monoclonal antibodies.
复制标题
流感神经氨酸酶与单克隆抗体复合的电子和 X 射线衍射研究。
DOI：
10.1016/0022-2836(86)90294-9
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发表时间：
1986
影响因子：
5.6
通讯作者：
Air,GM
中科院分区：
文献类型：
--
作者：
Tulloch,PA;Colman,PM;Davis,PC;Laver,WG;Webster,RG;Air,GM
流感病毒神经氨酸酶与抗原结合（Fab）片段和与整个单克隆抗体分子的复合物已经结晶。一个神经氨酸酶-Fab复合物（N9神经氨酸酶- nc35 Fab）的32/3 Fab和第二个神经氨酸酶-Fab复合物（N9神经氨酸酶- nc35 Fab）的较厚的晶体衍射x射线的分辨率约为4.0 Å，形成了适合电子衍射结构分析的均匀薄片状微晶体，反射分辨率约为4.3 Å。Fab和免疫球蛋白G与神经氨酸酶络合的微晶的电镜点阵图像已经根据各自的个别络合原体的负染色图像进行了解释。抗体与抗原的结合位点与神经氨酸酶单克隆变异中观察到的单个氨基酸变化发生在用于其选择的抗体的结合表位上的概念一致。
Complexes of influenza virus neuraminidase both with antigen-binding (Fab) fragments and with whole monoclonal antibody molecules have been crystallized. Uniformly thin platelet microcrystals suitable for structure analysis by electron diffraction, yielding reflections to approximately 4.3 Å resolution, have been grown from one neuraminidase-Fab complex, that of N9 neuraminidase with 32/3 Fab, and thicker crystals of a second neuraminidase-Fab complex (N9 neuraminidase-NC35 Fab) diffract X-rays to approximately 4.0 Å resolution. Electron microscope lattice images of microcrystals both of Fab and of immunoglobulin G complexed with neuraminidase have been interpreted in terms of negatively stained images of the respective individual complex protomers. The sites of binding of the antibodies to the antigen are consistent with the notion that single amino acid changes observed in monoclonal variants of neuraminidase occur in binding epitopes for the antibody used for their selection.