Dr. Yusuke Nakamichi, Mr. Kenta Tsutsumi, Dr. Akifumi Higashiura of Nakagawa Lab. and Dr. Naoyuki Miyazaki of Takagi Lab. and their collaborators revealed intermediate structure during self-assembly process of Rice dwarf virus using cryo-electron microscopy with phase plate.
Many viruses are covered with shells of
proteins that have an icosahedral structure which are known for the pattern of
a soccer ball. The Reoviridae viruses
have a distinctive structure further covered with a multilayered shell (capsid)
of a different pattern. Rotavirus that causes infant diarrhea is well known as
an example. We succeeded to reveal the formation of multilayered capsids with
different patterns in Rice Dwarf Virus
(RDV), one of the Reoviridae viruses,
by genetic engineering technology and phase-contrast cryo-electron microscopy.
RDV is covered with icosahedral capsids of
two different patterns called T = 1 (inner
shell) and T = 13 (outer capsid). In
this study, we coupled green fluorescent protein (GFP) to the outer capsid
protein using genetic recombination technology and used it to form virus
particles. As a result, RDV particles with an incomplete shell was created by the
sterically hinderance of GFP. A phase-contrast cryo-electron microscopy
revealed that the outer capsid proteins of RDV bind only to a specific region
of the inner capsid (on the three-fold axes). It was found that the outer shell
protein of RDV is firstly bound on the three-rotational axes of the inner
shell, and other pouter capsid proteins are sequentially inserted on the beside
of the initially bound proteins so as to combine the pieces of the puzzle.
This result revealed how the reovirus
particles with multilayered shells are formed for the first time. In addition, by
using this result to efficiently inhibit particle formation, it is expected to
be applicable to the prevention of infectious diseases and development of
This research project was conducted in
collaboration with Dr. Kazuyoshi Murata of National Institute for Physiological Sciences. Okazaki, Japan.
・Yoshinori Ohsumi （2016 Nobel Laureate, Honorary Professor, Tokyo Institute of Technology） ・Richard Henderson （2017 Nobel Laureate, MRC Laboratory of Molecular Biology) ・Bong-Jin Lee （Dean, College of Pharmacy, Seoul National University）
・Yoshihiro Yoneda （Director General and Project Leader, National Institutes of Biomedical Innovation, Health and Nutrition） ・Atsushi Miyawaki （Laboratory Head, RIKEN Center for Brain Science(CBS) ）
Institute for Protein Research, Osaka University
The Ministry of Education, Culture, Sports, Science and Technology (MEXT)announced the recipients of the 2018 Commendations for Science and Technology. From Osaka University, eight faculty member received awards, including Prof. Mariko Okada of Institute for Protein Research.
Prof. Okada was awarded the Prize for Science and Technology (Research Category).
Name of Achievement: Research on cellular mechanisms based on experiments and mathematical models
Assoc. Prof. Madoka Suzuki and his colleagues have been awarded a research grant (Program Grant) from the Human Frontier Science Program (HFSP) for their proposal, “Nanoscale heat transfer phenomena: new paradigm for intra- and intercellular signalling and shaping”.
On 4th January 2018, a paper has been published from Nucleic Acids Research (IF=10.162) by the research team of Dr. Kota Kasahara (Ritsumeikan University), Dr. Masaaki Shiina, Prof. Kazuhiro Ogata (Yokohama City University), Prof. Junichi Higo and Prof. Haruki Nakamura (IPR, Osaka University), revealing the regulation mechanism of the intrinsically disordered region of Ets1 transcription factor due to phosphorylation of Ser residues by molecular simulation and biochemical studies.
(The website linked from the title is displayed only in Japanese)
The aim of our exhibition is providing chances for various people to realize the diversity and importance of the “Shape” of proteins though experiences such as watching, feeling and constructing. We hope it helps them to deepen their understanding for biomolecules. The details of exhibition are as following:
“Watching” by accessing PDBj database and browsing protein molecules with CG in sterically.
“Feeling” by touching the molecule models made with a 3D printer
“Constructing” by making molecules with paper crafts
We also introduce the methods and facilities such as synchrotrons and high resolution electron microscopes (Nobel Prize of this year was awarded for it!) to solve molecule shapes.