3-DIMENSIONAL STRUCTURES OF INFLUENZA-VIRUS NEURAMINIDASE ANTIBODY COMPLEXES
3-DIMENSIONAL STRUCTURES OF INFLUENZA-VIRUS NEURAMINIDASE ANTIBODY COMPLEXES
复制标题
DOI：
10.1098/rstb.1989.0028
复制
发表时间：
1989-06-12
影响因子：
6.3
通讯作者：
WEBSTER, RG
中科院分区：
文献类型：
--
作者：
COLMAN, PM;TULIP, WR;WEBSTER, RG
与病毒抗原流感病毒神经氨酸酶结合的单克隆Fab片段NC 41的晶体的X射线衍射分析显示涉及抗原的五个表面环的表位。此外，它揭示了抗体可变模块中轻链和重链结构域之间的异常配对模式。我们将该结果解释为暗示与抗原的缔合可以通过可变轻链/可变重链（VL-VH）界面处的结构域的滑动来诱导Fab的四级结构的变化。此外，Fab结合改变了抗原的一些表面环的构象。NC 10 Fab-神经氨酸酶复合物的结构现在也已得到解决。其结合与NC 41表位重叠的表位。在这种结构中，Fab片段的C-模块没有电子密度，这意味着它在晶格中是无序的。这些和其他抗体抗原结构的影响，免疫识别进行了讨论。
X-ray diffraction analysis of crystals of a monoclonal Fab fragment NC41 bound to a viral antigen, influenza virus neuraminidase, shows an epitope involving five surface loops of the antigen. In addition it reveals and unusual pairing pattern between the domains of light and heavy chains in the variable module of the antibody. We interpret this result to imply that association with antigen can induce changes in the quaternary structure of the Fab, through a sliding of domains at the variable light/variable heavy chains (VL-VH) interface. In addition, Fab binding has altered the conformation of some of the surface loops of the antigen. The structure of the NC10 Fab-neuraminidase complex has now also been solved. It binds an epitope that overlaps the NC41 epitope. In this strucutre, there is no electron density for the C-module of the Fab fragment, implying it is disordered in the crystal lattice. The implications of these and other antibody-antigen structures, for immune recognition are discussed.