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Elucidating the mechanism of recognition and evasion in viral infection of tomato -Towards the development of new anti-viral agent– (Press Release)

Release Date
20 Aug, 2014
  • BL38B1 (Structural Biology III)

National Institute of Agrobiological Sciences
Osaka University
Iwate Medical University

   The structural basis in which the virus resistance protein found in wild tomato binds with the tomato mosaic virus protein to inhibit its propagation has been clarified. The virus resistance protein of tomato and the tomato mosaic virus protein each undergoes repetitive changes resulting in the host recognition of the viral molecule, viral adaptive evasion of the recognition, host counteradaptation, and viral response to counteradaptation. Such information on the structural basis of recognition and evasion could be used in developing an efficient plant anti-viral agent that can be expected to control the spread of viral diseases and an increase in the yield of affected crops.

Publication:
Kazuhiro Ishibashi, Yuichiro Kezuka, Chihoko Kobayashi, Masahiko Kato, Tsuyoshi Inoue, Takamasa Nonaka, Masayuki Ishikawa, Hiroyoshi Matsumura, Etsuko Katoh (2014)
"Structural Basis for the Recognition–Evasion Arms Race between Tomato mosaic virus and the Resistance Gene Tm-1."
Proceedings of the National Academy of Sciences of the United States of America. pnas.1407888111.

《Figures》

fig.1　A normal tomato (left) and transgenic tomato with Tm-1 gene (right) inoculated with tomato mosaic virus
Fig.1.  A normal tomato (left) and transgenic tomato with Tm-1 gene (right) inoculated with tomato mosaic virus.

 

Fig. 2. Structure of a complex of the helicase domain of tomato mosaic virus (ToMV) replication protein and Tm-1
Fig. 2.  Structure of a complex of the helicase domain of tomato mosaic virus (ToMV) replication protein and Tm-1.

The Tm-1 protein (colored blue and cyan) forms a dimer which binds with the ToMV helicase domain (colored pink and violet). An ATP molecule exists at the contact surface of each molecule.

Fig. 3. Co-evolution of ToMV-Hel protein and Tm-1
Fig. 3.  Co-evolution of ToMV-Hel protein and Tm-1.

(Left) Tm-1 binds with ToMV helicase to inhibit propagation of the virus. In this case, the Tm-1 amino acid no. 91 isoleucine (I91) interacts with the ToMV-Hel amino acid no. 979 glutamine (Q979) and no. 1097 aspartic acid (D1097). (Middle) Substitution of Q979 with glutamic acid (E979) allows ToMV to evade inhibitory interaction with Tm-1. (Right) Substitution of I91 with threonine (T91) in Tm-1 restores an interaction with E979, thereby inhibiting the propagation of the virus with E979 mutation.



For more information, please contact:
   Senior Researcher Etsuko Katoh
   (Biomolecular Research Unit, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan)
   E-mail：mail1