High-Resolution Cryo-Electron Microscopy Structures of Murine Norovirus 1 and Rabbit Hemorrhagic Disease Virus Reveal Marked Flexibility in the Receptor Binding Domains-Reference-Cited by-同舟云学术

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

Published:2010-06 Issue:11 Volume:84 Page:5836-5841
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Katpally Umesh¹,Voss Neil R.²,Cavazza Tommaso¹,Taube Stefan³,Rubin John R.⁴,Young Vivienne L.⁵,Stuckey Jeanne⁴,Ward Vernon K.⁵,Virgin Herbert W.⁶,Wobus Christiane E.³,Smith Thomas J.¹

Affiliation:

1. Donald Danforth Plant Science Center, 975 North Warson Road, Saint Louis, Missouri 63132

2. National Resource for Automated Molecular Microscopy, Scripps Research Institute, CB 129 10550 North Torrey Pines Road, La Jolla, California 92037

3. Department of Microbiology and Immunology, 5622 Medical Sciences Building II, 1150 West Medical Center Drive, University of Michigan Medical School, Ann Arbor, Michigan 48109

4. Life Science Institute, 210 Washtenaw Avenue, 3rd Floor, University of Michigan, Ann Arbor, Michigan 48109

5. Department of Microbiology and Immunology, School of Medical Sciences, University of Otago, P.O. Box 56, Dunedin 9054, New Zealand

6. Department of Molecular Microbiology, Washington University School of Medicine, Saint Louis, Missouri 63110

Abstract

ABSTRACT 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 ∼8-Å 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.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JVI.00314-10

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