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Your search keyword '"Kimura, Kanako Terakado"' showing total 3 results
Start Over Author "Kimura, Kanako Terakado" Publication Type Electronic Resources
3 results on '"Kimura, Kanako Terakado"'

1. Virological characteristics of the SARS-CoV-2 Omicron XBB.1.5 variant

Author

50632098, 10759509, Tamura, Tomokazu, Irie, Takashi, Deguchi, Sayaka, Yajima, Hisano, Tsuda, Masumi, Nasser, Hesham, Mizuma, Keita, Plianchaisuk, Arnon, Suzuki, Saori, Uriu, Keiya, Begum, Mst Monira, Shimizu, Ryo, Jonathan, Michael, Suzuki, Rigel, Kondo, Takashi, Ito, Hayato, Kamiyama, Akifumi, Yoshimatsu, Kumiko, Shofa, Maya, Hashimoto, Rina, Anraku, Yuki, Kimura, Kanako Terakado, Kita, Shunsuke, Sasaki, Jiei, Sasaki-Tabata, Kaori, Maenaka, Katsumi, Nao, Naganori, Wang, Lei, Oda, Yoshitaka, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Ikeda, Terumasa, Saito, Akatsuki, Matsuno, Keita, Ito, Jumpei, Tanaka, Shinya, Sato, Kei, Hashiguchi, Takao, Takayama, Kazuo, Fukuhara, Takasuke, 50632098, 10759509, Tamura, Tomokazu, Irie, Takashi, Deguchi, Sayaka, Yajima, Hisano, Tsuda, Masumi, Nasser, Hesham, Mizuma, Keita, Plianchaisuk, Arnon, Suzuki, Saori, Uriu, Keiya, Begum, Mst Monira, Shimizu, Ryo, Jonathan, Michael, Suzuki, Rigel, Kondo, Takashi, Ito, Hayato, Kamiyama, Akifumi, Yoshimatsu, Kumiko, Shofa, Maya, Hashimoto, Rina, Anraku, Yuki, Kimura, Kanako Terakado, Kita, Shunsuke, Sasaki, Jiei, Sasaki-Tabata, Kaori, Maenaka, Katsumi, Nao, Naganori, Wang, Lei, Oda, Yoshitaka, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Ikeda, Terumasa, Saito, Akatsuki, Matsuno, Keita, Ito, Jumpei, Tanaka, Shinya, Sato, Kei, Hashiguchi, Takao, Takayama, Kazuo, and Fukuhara, Takasuke

Abstract

Circulation of SARS-CoV-2 Omicron XBB has resulted in the emergence of XBB.1.5, a new Variant of Interest. Our phylogenetic analysis suggests that XBB.1.5 evolved from XBB.1 by acquiring the S486P spike (S) mutation, subsequent to the acquisition of a nonsense mutation in ORF8. Neutralization assays showed similar abilities of immune escape between XBB.1.5 and XBB.1. We determine the structural basis for the interaction between human ACE2 and the S protein of XBB.1.5, showing similar overall structures between the S proteins of XBB.1 and XBB.1.5. We provide the intrinsic pathogenicity of XBB.1 and XBB.1.5 in hamsters. Importantly, we find that the ORF8 nonsense mutation of XBB.1.5 resulted in impairment of MHC suppression. In vivo experiments using recombinant viruses reveal that the XBB.1.5 mutations are involved with reduced virulence of XBB.1.5. Together, our study identifies the two viral functions defined the difference between XBB.1 and XBB.1.5.

Published
2024

2. Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant

Author

80833334, 10759509, 50632098, Ito, Jumpei, Suzuki, Rigel, Uriu, Keiya, Itakura, Yukari, Zahradnik, Jiri, Kimura, Kanako Terakado, Deguchi, Sayaka, Wang, Lei, Lytras, Spyros, Tamura, Tomokazu, Kida, Izumi, Nasser, Hesham, Shofa, Maya, Begum, Mst Monira, Tsuda, Masumi, Oda, Yoshitaka, Suzuki, Tateki, Sasaki, Jiei, Sasaki-Tabata, Kaori, Fujita, Shigeru, Yoshimatsu, Kumiko, Ito, Hayato, Nao, Naganori, Asakura, Hiroyuki, Nagashima, Mami, Sadamasu, Kenji, Yoshimura, Kazuhisa, Yamamoto, Yuki, Nagamoto, Tetsuharu, Kuramochi, Jin, Schreiber, Gideon, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Saito, Akatsuki, Matsuno, Keita, Takayama, Kazuo, Hashiguchi, Takao, Tanaka, Shinya, Fukuhara, Takasuke, Ikeda, Terumasa, Sato, Kei, 80833334, 10759509, 50632098, Ito, Jumpei, Suzuki, Rigel, Uriu, Keiya, Itakura, Yukari, Zahradnik, Jiri, Kimura, Kanako Terakado, Deguchi, Sayaka, Wang, Lei, Lytras, Spyros, Tamura, Tomokazu, Kida, Izumi, Nasser, Hesham, Shofa, Maya, Begum, Mst Monira, Tsuda, Masumi, Oda, Yoshitaka, Suzuki, Tateki, Sasaki, Jiei, Sasaki-Tabata, Kaori, Fujita, Shigeru, Yoshimatsu, Kumiko, Ito, Hayato, Nao, Naganori, Asakura, Hiroyuki, Nagashima, Mami, Sadamasu, Kenji, Yoshimura, Kazuhisa, Yamamoto, Yuki, Nagamoto, Tetsuharu, Kuramochi, Jin, Schreiber, Gideon, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Saito, Akatsuki, Matsuno, Keita, Takayama, Kazuo, Hashiguchi, Takao, Tanaka, Shinya, Fukuhara, Takasuke, Ikeda, Terumasa, and Sato, Kei

Abstract

In late 2022, various Omicron subvariants emerged and cocirculated worldwide. These variants convergently acquired amino acid substitutions at critical residues in the spike protein, including residues R346, K444, L452, N460, and F486. Here, we characterize the convergent evolution of Omicron subvariants and the properties of one recent lineage of concern, BQ.1.1. Our phylogenetic analysis suggests that these five substitutions are recurrently acquired, particularly in younger Omicron lineages. Epidemic dynamics modelling suggests that the five substitutions increase viral fitness, and a large proportion of the fitness variation within Omicron lineages can be explained by these substitutions. Compared to BA.5, BQ.1.1 evades breakthrough BA.2 and BA.5 infection sera more efficiently, as demonstrated by neutralization assays. The pathogenicity of BQ.1.1 in hamsters is lower than that of BA.5. Our multiscale investigations illuminate the evolutionary rules governing the convergent evolution for known Omicron lineages as of 2022.

Published
2023

3. Structure of the bile acid transporter and HBV receptor NTCP

Author

Asami, Jinta, Kimura, Kanako Terakado, Fujita-Fujiharu, Yoko, Ishida, Hanako, Zhang, Zhikuan, Nomura, Yayoi, Liu, Kehong, Uemura, Tomoko, Sato, Yumi, Ono, Masatsugu, Yamamoto, Masaki, Noda, Takeshi, Shigematsu, Hideki, Drew, David, Iwata, So, Shimizu, Toshiyuki, Nomura, Norimichi, Ohto, Umeharu, Asami, Jinta, Kimura, Kanako Terakado, Fujita-Fujiharu, Yoko, Ishida, Hanako, Zhang, Zhikuan, Nomura, Yayoi, Liu, Kehong, Uemura, Tomoko, Sato, Yumi, Ono, Masatsugu, Yamamoto, Masaki, Noda, Takeshi, Shigematsu, Hideki, Drew, David, Iwata, So, Shimizu, Toshiyuki, Nomura, Norimichi, and Ohto, Umeharu

Abstract

Chronic infection with hepatitis B virus (HBV) affects more than 290 million people worldwide, is a major cause of cirrhosis and hepatocellular carcinoma, and results in an estimated 820,000 deaths annually. For HBV infection to be established, a molecular interaction is required between the large glycoproteins of the virus envelope (known as LHBs) and the host entry receptor sodium taurocholate co-transporting polypeptide (NTCP), a sodium-dependent bile acid transporter from the blood to hepatocytes. However, the molecular basis for the virus–transporter interaction is poorly understood. Here we report the cryo-electron microscopy structures of human, bovine and rat NTCPs in the apo state, which reveal the presence of a tunnel across the membrane and a possible transport route for the substrate. Moreover, the cryo-electron microscopy structure of human NTCP in the presence of the myristoylated preS1 domain of LHBs, together with mutation and transport assays, suggest a binding mode in which preS1 and the substrate compete for the extracellular opening of the tunnel in NTCP. Our preS1 domain interaction analysis enables a mechanistic interpretation of naturally occurring HBV-insusceptible mutations in human NTCP. Together, our findings provide a structural framework for HBV recognition and a mechanistic understanding of sodium-dependent bile acid translocation by mammalian NTCPs.

Published
2022
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