High-Resolution Cryo-Electron Microscopy Structures of Murine Norovirus 1 and Rabbit Hemorrhagic Disease Virus Reveal Marked Flexibility in the Receptor Binding Domains

被引:61
作者
Katpally, Umesh [1 ]
Voss, Neil R. [2 ]
Cavazza, Tommaso [1 ]
Taube, Stefan [3 ]
Rubin, John R. [5 ]
Young, Vivienne L. [4 ]
Stuckey, Jeanne [5 ]
Ward, Vernon K. [4 ]
Virgin, Herbert W. [6 ]
Wobus, Christiane E. [3 ]
Smith, Thomas J. [1 ]
机构
[1] Donald Danforth Plant Sci Ctr, St Louis, MO 63132 USA
[2] Scripps Res Inst, La Jolla, CA 92037 USA
[3] Univ Michigan, Sch Med, Dept Microbiol & Immunol, Ann Arbor, MI 48109 USA
[4] Univ Otago, Sch Med Sci, Dept Microbiol Immunol, Dunedin 9054, New Zealand
[5] Univ Michigan, Inst Life Sci, Ann Arbor, MI 48109 USA
[6] Washington Univ, Sch Med, Dept Mol Microbiol, St Louis, MO 63110 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1128/JVI.00314-10
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the three-dimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to similar to 8-angstrom resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.
引用
收藏
页码:5836 / 5841
页数:6
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