Biophysical Reviews

, Volume 10, Issue 2, pp 659–665 | Cite as

Hierarchical structure assembly model of rice dwarf virus particle formation

  • Atsushi Nakagawa
  • Naoyuki Miyazaki
  • Akifumi Higashiura
Review
  • 140 Downloads

Abstract

Rice dwarf virus (RDV) of the family Reoviridae and genus Phytoreovirus, is the cause of rice dwarf disease, a major negative effector of rice production throughout East Asia, including Japan. RDV has an icosahedral double-layered shell of approximately 70 nm diameter. The structural proteins constituting the capsid can self-assemble into a correct particle without requiring the help of any external factors in vitro. A total of more than 900 components assemble to make the full particle. A series of structural and functional studies of RDV, including X-ray crystallography and cryo-electron microscopy, suggest a hierarchical self-assembly mechanism involving both homologous and heterologous interactions. As such, systems for the recognition of each component should be essential for particle formation.

Keywords

Virus assembly Multi-layered virus Reoviridae Rice dwarf virus Capsid structure 

Notes

Acknowledgements

The authors thank to Dr. Toshihiro Omura of the National Agricultural Research Center and Prof. Tomitake Tsukihara of the University of Hyogo for their continuous support and encouragement for the structural studies of rice dwarf virus project. This study was partly supported by the collaborative research program of National Institute for Physiological Sciences.

Compliance with ethical standards

Conflict of interest

Atsushi Nakagawa declares that he has no conflicts of interest. Naoyuki Miyazaki declares that he has no conflicts of interest. Akifumi Higashiura declares that he has no conflicts of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

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Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  1. 1.Institute for Protein ResearchOsaka UniversitySuitaJapan

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