Takahide Kouno
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Takahide Kouno has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Hiroshi Matsuo
Cancer Innovation Laboratory, Frederick National Laboratory for Cancer Research, Frederick, USA
1 shared publication - Jaekyung Hyun
School of Pharmacy, Sungkyunkwan University, Suwon, Republic of Korea
1 shared publication - Matthias Wolf
Molecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan
1 shared publication - Megumi Shigematsu
Computational Medicine Center, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, USA
1 shared publication - Satoshi Shibata
Molecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan
1 shared publication Tae Gyun Kim
Molecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Onna-son, Japan
1 shared publication
Latest Publications
- Open Access
- 7 July 2023
- Published by Springer Nature in Nature Communications
- Vol. 14 (1) , 1-14
Structural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G
Great effort has been devoted to discovering the basis of A3G-Vif interaction, the key event of HIV’s counteraction mechanism to evade antiviral innate immune response. Here we show reconstitution of the A3G-Vif complex and subsequent A3G ubiquitination in vitro and report the cryo-EM structure of the A3G-Vif complex at 2.8 Å resolution using solubility-enhanced variants of A3G and Vif. We present an atomic model of the A3G-Vif interface, which assembles via known amino acid determinants. This assembly is not achieved by protein-protein interaction alone, but also involves RNA. The cryo-EM structure and in vitro ubiquitination assays identify an adenine/guanine base preference for the interaction and a unique Vif-ribose contact. This establishes the biological significance of an RNA ligand. Further assessment of interactions between A3G, Vif, and RNA ligands show that the A3G-Vif assembly and subsequent ubiquitination can be controlled by amino acid mutations at the interface or by polynucleotide modification, suggesting that a specific chemical moiety would be a promising pharmacophore to inhibit the A3G-Vif interaction.
- 7 July 2023
- Published by Springer Nature in Nature Communications
- Vol. 14 (1) , 1-14
Open AccessStructural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G
Great effort has been devoted to discovering the basis of A3G-Vif interaction, the key event of HIV’s counteraction mechanism to evade antiviral innate immune response. Here we show reconstitution of the A3G-Vif complex and subsequent A3G ubiquitination in vitro and report the cryo-EM structure of the A3G-Vif complex at 2.8 Å resolution using solubility-enhanced variants of A3G and Vif. We present an atomic model of the A3G-Vif interface, which assembles via known amino acid determinants. This assembly is not achieved by protein-protein interaction alone, but also involves RNA. The cryo-EM structure and in vitro ubiquitination assays identify an adenine/guanine base preference for the interaction and a unique Vif-ribose contact. This establishes the biological significance of an RNA ligand. Further assessment of interactions between A3G, Vif, and RNA ligands show that the A3G-Vif assembly and subsequent ubiquitination can be controlled by amino acid mutations at the interface or by polynucleotide modification, suggesting that a specific chemical moiety would be a promising pharmacophore to inhibit the A3G-Vif interaction.