Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins

被引:284
作者
Lok, Shee-Mei [1 ]
Kostyuchenko, Victor [1 ]
Nybakken, Grant E. [2 ]
Holdaway, Heather A. [1 ]
Battisti, Anthony J. [1 ]
Sukupolvi-Petty, Soila [3 ]
Sedlak, Dagmar [1 ]
Fremont, Daved H. [2 ]
Chipman, Paul R. [1 ]
Roehrig, John T. [4 ]
Diamond, Michael S. [2 ,3 ,5 ]
Kuhn, Richard J. [1 ]
Rossmann, Michael G. [1 ]
机构
[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
[2] Washington Univ, Sch Med, Dept Pathol & Immunol, St Louis, MO 63110 USA
[3] Washington Univ, Sch Med, Dept Med, St Louis, MO 63110 USA
[4] Ctr Dis Control & Prevent, Arbovirus Dis Branch, Div Vector Borne Infect Dis, Publ Hlth Serv,US Dept Hlth & Human Serv, Ft Collins, CO 80522 USA
[5] Washington Univ, Sch Med, Dept Mol Microbiol, St Louis, MO 63110 USA
关键词
D O I
10.1038/nsmb.1382
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The monoclonal antibody 1A1D-2 has been shown to strongly neutralize dengue virus serotypes 1, 2 and 3, primarily by inhibiting attachment to host cells. A crystal structure of its antigen binding fragment (Fab) complexed with domain III of the viral envelope glycoprotein, E, showed that the epitope would be partially occluded in the known structure of the mature dengue virus. Nevertheless, antibody could bind to the virus at 37 degrees C, suggesting that the virus is in dynamic motion making hidden epitopes briefly available. A cryo-electron microscope image reconstruction of the virus: Fab complex showed large changes in the organization of the E protein that exposed the epitopes on two of the three E molecules in each of the 60 icosahedral asymmetric units of the virus. The changes in the structure of the viral surface are presumably responsible for inhibiting attachment to cells.
引用
收藏
页码:312 / 317
页数:6
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