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Kaori Tabata Last modified date:2024.04.09

Assistant Professor / Division of Molecular Bioinformatics
Department of Chemo-Pharmaceutical Sciences
Faculty of Pharmaceutical Sciences


Graduate School
Undergraduate School


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Homepage
https://kyushu-u.elsevierpure.com/en/persons/kaori-tabata
 Reseacher Profiling Tool Kyushu University Pure
Academic Degree
Ph.D.
Country of degree conferring institution (Overseas)
No
Field of Specialization
molecular biology, protein science
Total Priod of education and research career in the foreign country
02years00months
Research
Research Interests
  • Development of the prevention and the therapeutic drug for COVID-19
    keyword : COVID-19
    2021.06~2025.06.
  • The role of exosome in the cell-cell communication
    keyword : exosome
    2019.04~2024.06.
  • Posttranslational regulation of CRF2 and impact on plant growth and development
    keyword : cytokinin response factor
    2017.04~2022.03.
  • Structural Basis for synthesis of tropane by polyketide synthase from Datura
    keyword : polyketide synthase
    2014.04.
  • Studies on the mechanism of cell death induced by cannabinoids
    keyword : cell death
    2013.01.
  • Structure and function analysis of heparanase involved in cancer metastasis
    keyword : structural analysis
    2010.06.
  • Silkworm expression of immune cell surface receptor
    keyword : protein science
    2007.04.
  • Structure and function of DNA replication related protein in Escherichia coli
    keyword : structural analysis
    2003.04.
  • Studies on the metabolic enzyme from medicinal plants
    keyword : enzyme, cloning
    2000.04.
Academic Activities
Papers
1. Tamura T, Ito J, Uriu K, Zahradnik J, Kida I, Anraku Y, Nasser H, Shofa M, Oda Y, Lytras S, Nao N, Itakura Y, Deguchi S, Suzuki R, Wang L, Begum MM, Kita S, Yajima H, Sasaki J, Sasaki-Tabata K, Shimizu R, Tsuda M, Kosugi Y, Fujita S, Pan L, Sauter D, Yoshimatsu K, Suzuki S, Asakura H, Nagashima M, Sadamasu K, Yoshimura K, Yamamoto Y, Nagamoto T, Schreiber G, Maenaka K; Genotype to Phenotype Japan (G2P-Japan) Consortium; Hashiguchi T, Ikeda T, Fukuhara T, Saito A, Tanaka S, Matsuno K, Takayama K, Sato K., Virological characteristics of the SARS-CoV-2 XBB variant derived from recombination of two Omicron subvariants., Nat Commun., 16, 14(1), 2800, 2023.05.
2. Ito J, Suzuki R, Uriu K, Itakura Y, Zahradnik J, Kimura KT, Deguchi S, Wang L, Lytras S, Tamura T, Kida I, Nasser H, Shofa M, Begum MM, Tsuda M, Oda Y, Suzuki T, Sasaki J, Sasaki-Tabata K, Fujita S, Yoshimatsu K, Ito H, Nao N, Asakura H, Nagashima M, Sadamasu K, Yoshimura K, Yamamoto Y, Nagamoto T, Kuramochi J, Schreiber G; Genotype to Phenotype Japan (G2P-Japan) Consortium; Saito A, Matsuno K, Takayama K, Hashiguchi T, Tanaka S, Fukuhara T, Ikeda T, Sato K., Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant., Nat Commun., 10.1038/s41467-023-38188-, 14, 1, 2671, 2023.05.
3. Saito, Akatsuki; Tamura, Tomokazu; Zahradnik, Jiri; Deguchi, Sayaka; Tabata, Koshiro; Anraku, Yuki; Kimura, Izumi; Ito, Jumpei; Yamasoba, Daichi; Nasser, Hesham; Toyoda, Mako; Nagata, Kayoko; Uriu, Keiya; Kosugi, Yusuke; Fujita, Shigeru; Shofa, Maya; Begum, Mst Monira; Shimizu, Ryo; Oda, Yoshitaka; Suzuki, Rigel; Ito, Hayato; Nao, Naganori; Wang, Lei; Tsuda, Masumi; Yoshimatsu, Kumiko; Kuramochi, Jin; Kita, Shunsuke; Sasaki-Tabata, Kaori; Fukuhara, Hideo; Maenaka, Katsumi; Yamamoto, Yuki; Nagamoto, Tetsuharu; Asakura, Hiroyuki; Nagashima, Mami; Sadamasu, Kenji; Yoshimura, Kazuhisa; Ueno, Takamasa; Schreiber, Gideon; Takaori-Kondo, Akifumi; Shirakawa, Kotaro; Sawa, Hirofumi; Irie, Takashi; Hashiguchi, Takao; Takayama, Kazuo; Matsuno, Keita; Tanaka, Shinya; Ikeda, Terumasa; Fukuhara, Takasuke; Sato, Kei, Virological characteristics of the SARS-CoV-2 Omicron BA.2.75 variant, CELL HOST & MICROBE, 10.1016/j.chom.2022.10.003, 30, 9, 1540, 2022.09.
4. Izumi Kimura, Daichi Yamasoba, Tomokazu Tamura, Naganori Nao, Tateki Suzuki, Yoshitaka Oda, Shuya Mitoma, Jumpei Ito, Hesham Nasser, Jiri Zahradnik, Keiya Uriu, Shigeru Fujita, Yusuke Kosugi, Lei Wang, Masumi Tsuda, Mai Kishimoto, Hayato Ito, Rigel Suzuki, Ryo Shimizu, M.S.T. Monira Begum, Kumiko Yoshimatsu, Kanako Terakado Kimura, Jiei Sasaki, Kaori Sasaki-Tabata, Yuki Yamamoto, Tetsuharu Nagamoto, Jun Kanamune, Kouji Kobiyama, Hiroyuki Asakura, Mami Nagashima, Kenji Sadamasu, Kazuhisa Yoshimura, Kotaro Shirakawa, Akifumi Takaori-Kondo, Jin Kuramochi, Gideon Schreiber, Ken J. Ishii, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Takao Hashiguchi, Terumasa Ikeda, Akatsuki Saito, Takasuke Fukuhara, Shinya Tanaka, Keita Matsuno, Kei Sato, Virological characteristics of the SARS-CoV-2 Omicron BA.2 subvariants including BA.4 and BA.5, Cell, 10.1016/j.cell.2022.09.018, 185, 21, 3992-4007, 2022.10, After the global spread of the SARS-CoV-2 Omicron BA.2, some BA.2 subvariants, including BA.2.9.1, BA.2.11, BA.2.12.1, BA.4, and BA.5, emerged in multiple countries. Our statistical analysis showed that the effective reproduction numbers of these BA.2 subvariants are greater than that of the original BA.2. Neutralization experiments revealed that the immunity induced by BA.1/2 infections is less effective against BA.4/5. Cell culture experiments showed that BA.2.12.1 and BA.4/5 replicate more efficiently in human alveolar epithelial cells than BA.2, and particularly, BA.4/5 is more fusogenic than BA.2. We further provided the structure of the BA.4/5 spike receptor-binding domain that binds to human ACE2 and considered how the substitutions in the BA.4/5 spike play roles in ACE2 binding and immune evasion. Moreover, experiments using hamsters suggested that BA.4/5 is more pathogenic than BA.2. Our multiscale investigations suggest that the risk of BA.2 subvariants, particularly BA.4/5, to global health is greater than that of original BA.2..
5. Sasaki K, Taura F, Shoyama Y, Morimoto S, Molecular characterization of a novel beta-glucuronidase from Scutellaria baicalensis georgi, J. Biol. Chem., 275, 35, 27466-27472, 2000.09.
6. Sasaki K, Ose T, Tanaka T, Mizukoshi T, Ishigaki T, Maenaka K, Masai H, Kohda D, Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli, Biochim. Biophys. Acta, 1764, 1, 157-160 , 2006.01.
7. Sasaki K, Ose T, Okamoto N, Maenaka K, Tanaka T, Masai H, Saito M, Shirai T, Kohda D, Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA, EMBO J., 26, 10, 2584-2593 , 2007.05.
8. Sasaki K, Kajikawa M, Kuroki K, Motohashi T, Shimojima T, Park EY, Kondo S, Yagi H, Kato K, Maenaka K, Silkworm expression and sugar profiling of human immune cell surface receptor, KIR2DL1, Biochem. Biophys. Res. Commun., 387, 3, 575-580 , 2009.09.
Presentations
1. Sasaki-Tabata K, Matsuo A, Fuchida H, Ojida A, Tanaka H and Morimoto S, Cloning, expression and characterization of polyketide synthase gene from Scopolia Japonica, The 9th CSP-KSP-JSP Joint Symposium on Pharmacognosy, 2016.05, BACKGROUND AND PURPOSE: Various important pharmacological compounds such as atropine and scopolamine are included in Scopolia japonica. These compounds are synthesized using ornithine as a starting material, however, it’s unclear which enzyme catalyzes the tropinone synthesis reaction. Hence, in the present study we aimed to identify function and structure of novel polyketide synthase (PKS) from S. japonica.
EXPERIMENTAL APPROACH: A total RNA was extracted from leaves of S. japonica and cDNA was synthesized using a reverse transcriptase. Then, degenerate PCR, 5' and 3' RACE was performed using cDNA as a template. Two novel genes were obtained and expressed in E. coli. The recombinant protein was purified with affinity column and ion exchange column. We analyzed the enzyme activity using HPLC. Moreover, we crystallized and performed crystallographic analysis of PKS.
KEY RESULTS: Two novel genes of PKS from S. japonica were obtained. The recombinant PKSs expressed in E. coli as a soluble fraction was highly purified using affinity and ion exchange column and the enzyme assay with HPLC showed that new compounds were synthesized using some substrates. Moreover, crystallization screening resulted in obtaining needle or plate crystals. We could get single crystals in an optimized condition. The crystal diffracted to 2.0 angstrom at KEK-PF and the structures of PKS were determined using molecular replacement method.
CONCLUSION AND IMPLICATIONS: These PKS genes seem to belong to PKS family because they showed high similarity to other CHS from various plants. These novel findings may contribute to clarifying the mechanism of tropane synthesis..
Membership in Academic Society
  • The Pharmaceutical Society of Japan
  • The Japanese Society of Pharmacognosy
  • The Molecular Biology Society of Japan