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京都大学 医生物学研究所 ウイルス制御分野 教授
橋口 隆生 Takao Hashiguchi

学歴・職歴

2022年 京都大学 医生物学研究所 ウイルス制御分野・教授
2020年 京都大学 ウイルス・再生医科学研究所 ウイルス制御分野・教授
2016年 九州大学大学院 医学研究院 ウイルス学・准教授
2013年 九州大学大学院 医学研究院 ウイルス学・助教
2010年 The Scripps Research Institute (USA)
2010-2012年　日本学術振興会 海外特別研究員
2012-2013年　上原記念生命科学財団 リサーチフェロー
2008年 九州大学大学院 医学研究院 ウイルス学・日本学術振興会 特別研究員（PD）
2008年 九州大学大学院 医学系学府 博士課程 病態医学専攻 早期修了
2005年 九州大学大学院 医学系学府 修士課程 医科学専攻 修了
2003年 九州大学 理学部 化学科 卒業

学位

2008年 博士（医学）（九州大学）

所属学会

日本ウイルス学会、日本蛋白質科学会、米国微生物学会

受賞歴

2016年 文部科学大臣表彰 若手科学者賞
2016年 日本ウイルス学会 杉浦奨励賞
2016年 第一回 日本医療研究開発大賞 AMED理事長賞受賞

論文（英文）

以下のリンクを参照
http://www.ncbi.nlm.nih.gov/pubmed/?term=takao+hashiguchi

主要論文

  1. Gao Z, Sasaki J, Suzuki T, Suzuki T, Miwa Y, Sando S, *Hashiguchi T, *Morimoto J. Discovery of potent measles virus fusion inhibitor peptides via structure-guided derivatization. RSC Med Chem. 2025 Jan 24. doi: 10.1039/d4md01006j.
  2. Sasaki J, Sato A, Sasaki M, Okabe I, Kodama K, Otsuguro S, Yasuda K, Kojima H, Orba Y, Sawa H, Maenaka K, Yanagi Y, *Hashiguchi T. X-206 exhibits broad-spectrum anti-β-coronavirus activity, covering SARS-CoV-2 variants and drug-resistant isolates. Antiviral Res. 2024 19;232:106039. doi: 10.1016/j.antiviral.2024.106039.
  3. Yajima H, Anraku Y, Kaku Y, Kimura KT, Plianchaisuk A, Okumura K, Nakada-Nakura Y, Atarashi Y, Hemmi T, Kroda D, Takahashi Y, Kita S, Sasaki J, Sumita H, ; Genotype to Phenotype Japan (G2P-Japan) Consortium; Ito J, Maenaka K, *Sato K, *Hashiguchi T. Structural basis for receptor-binding domain mobility of the spike in SARS-CoV-2 BA.2.86 and JN.1. Nat Commun 15, 8574 (2024). https://doi.org/10.1038/s41467-024-52808-2
  4. Yajima H, Nomai T, Okumura K, Maenaka K, , Ito J, *Hashiguchi T, *Sato K. Molecular and structural insights into SARS-CoV-2 evolution: from BA.2 to XBB subvariants. mBio 0:e03220-23. https://doi.org/10.1128/mbio.03220-23
  5. Tamura T, Irie T, Deguchi S, Yajima H, Tsuda M, Nasser H, Mizuma K, Plianchaisuk A, Suzuki S, Uriu K, Begum MM, Shimizu R, Jonathan M, Suzuki R, Kondo T, Ito H, Kamiyama A, Yoshimatsu K, Shofa M, Hashimoto R, Anraku Y, Kimura KT, Kita S, Sasaki J, Sasaki-Tabata K, Maenaka K, Nao N, Wang L, Oda Y; Genotype to Phenotype Japan (G2P-Japan) Consortium; Ikeda T, Saito A, Matsuno K, Ito J, *Tanaka S, *Sato K, *Hashiguchi T, *Takayama K, *Fukuhara T. Virological characteristics of the SARS-CoV-2 Omicron XBB.1.5 variant. Nat Commun. 2024 Feb 8;15(1):1176. doi: 10.1038/s41467-024-45274-3.  
  6. Tonouchi K, Adachi Y, Suzuki T, Kuroda D, Nishiyama A, Yumoto K, Takeyama H, Suzuki T, Hashiguchi T, *Takahashi Y. Structural basis for cross-group recognition of an influenza virus hemagglutinin antibody that targets postfusion stabilized epitope. PLoS Pathog. 2023 Aug 9;19(8):e1011554. doi: 10.1371/journal.ppat.1011554. 
  7. Moriyama S, Anraku Y, Taminishi S, Adachi Y, Kuroda D, Kita S, Higuchi Y, Kirita Y, Kotaki R, Tonouchi K, Yumoto K, Suzuki T, Someya T, Fukuhara H, Kuroda Y, Yamamoto T, Onodera T, Fukushi S, Maeda K, Nakamura-Uchiyama F, Hashiguchi T, Hoshino A, Maenaka K, *Takahashi Y. Structural delineation and computational design of SARS-CoV-2-neutralizing antibodies against Omicron subvariants. Nat Commun. 2023 Jul 14;14(1):4198. doi: 10.1038/s41467-023-39890-8.
  8. 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. 2023 May 16;14(1):2800. doi: 10.1038/s41467-023-38435-3.
  9. 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. 2023 May 11;14(1):2671. doi: 10.1038/s41467-023-38188-z.
  10. *Shirogane Y, Harada H, Hirai Y, Takemoto R, Suzuki T, Hashiguchi T, Yanagi Y. Collective fusion activity determines neurotropism of an en bloc transmitted enveloped virus. Sci Adv. 2023 Jan 27;9(4):eadf3731. doi: 10.1126/sciadv.adf3731.
  11. Saito A, Tamura T, Zahradnik J, Deguchi S, Tabata K, Anraku Y, Kimura I, Ito J, Yamasoba D, Nasser H, Toyoda M, Nagata K, Uriu K, Kosugi Y, Fujita S, Shofa M, Monira Begum M, Shimizu R, Oda Y, Suzuki R, Ito H, Nao N, Wang L, Tsuda M, Yoshimatsu K, Kuramochi J, Kita S, Sasaki-Tabata K, Fukuhara H, Maenaka K, Yamamoto Y, Nagamoto T, Asakura H, Nagashima M, Sadamasu K, Yoshimura K, Ueno T, Schreiber G, Takaori-Kondo A; Genotype to Phenotype Japan (G2P-Japan) Consortium; Shirakawa K, Sawa H, Irie T, Hashiguchi T, Takayama K, Matsuno K, *Tanaka S, *Ikeda T, *Fukuhara T, *Sato K. Virological characteristics of the SARS-CoV-2 Omicron BA.2.75 variant. Cell Host Microbe. 2022 Nov 9;30(11):1540-1555.e15. doi: 10.1016/j.chom.2022.10.003.
  12. Kimura I, Yamasoba D, Tamura T, Nao N, Suzuki T, Oda Y, Mitoma S, Ito J, Nasser H, Zahradnik J, Uriu K, Fujita S, Kosugi Y, Wang L, Tsuda M, Kishimoto M, Ito H, Suzuki R, Shimizu R, M.S.T. Begum M, Yoshimatsu K, Kimura KT, Sasaki J, Tabata KS, Yamamoto Y, Nagamoto Y, Kanamune J, Kobiyama K, Asakura H, Nagashima M, Sadamasu K, Yoshimura K, Shirakawa K, Kondo AT, Kuramochi J, Schreiber G, Ishii KJ, *Hashiguchi T, *Ikeda T, *Saito A, *Fukuhara T, *Tanaka S, *Matsuno K, *Sato K. Virological characteristics of the SARS-CoV-2 Omicron BA.2 subvariants including BA.4 and BA.5.
    Cell. 2022. doi: 10.1016/j.cell.2022.09.018
  13. Onodera T, Kita S, Adachi Y, Moriyama S, Sato A, Nomura T, Sakakibara S, Inoue T, Tadokoro T, Anraku Y, Yumoto K, Tian G, Fukuhara H, Sasaki M, Orba Y, Shiwa N, Iwata N, Nagata N, Suzuki T, Sasaki J, Sekizuka T, Tonouchi K, Fukushi S, Satofuka H, Kazuki Y, Sun L, Oshimura M, Kurosaki T, Kuroda M, Matsuura Y, Suzuki T, Sawa H, Hashiguchi T, *Maenaka K, and *Takahashi Y. A SARS-CoV-2 Antibody Broadly Neutralizes SARS-related Coronaviruses and Variants by Coordinated Recognition of a Virus Vulnerable Site. 
    Immunity. 2021 Oct 12;54(10):2385-2398.e10. doi: 10.1016/j.immuni.2021.08.025.
  14. Ikegame S, Hashiguchi T, Hung CT, Dobrindt K, Brennand KJ, Takeda M, *Lee B. Fitness selection of hyperfusogenic measles virus F proteins associated with neuropathogenic phenotypes.                                                                                                    Proc Natl Acad Sci U S A 2021 May 4;118(18):e2026027118.
  15. Kubota M, Okabe I, Nakakita SI, Ueo A, Shirogane Y, Yanagi Y, *Hashiguchi T. Disruption of the Dimer-Dimer Interaction of the Mumps Virus Attachment Protein Head Domain, Aided by an Anion Located at the Interface, Compromises Membrane Fusion Triggering.
    J Virol. 2020;94(2). pii: e01732-19. p1-11.
  16. Kubota M, Matsuoka R, Suzuki T, Yonekura K, Yanagi Y, *Hashiguchi T. Molecular Mechanism of the Flexible Glycan Receptor Recognition by Mumps Virus.
    J Virol. 2019;93(15). pii: e00344-19. p1-13.
  17. *Hashiguchi T, Fukuda Y, Matsuoka R, Kuroda D, Kubota M, Shirogane Y, Watanabe S, Tsumoto K, Kohda D, Plemper RK, *Yanagi Y. Structures of the prefusion form of measles virus fusion protein in complex with inhibitors.
    Proc Natl Acad Sci U S A. 2018;115(10):2496-501.
  18. Kubota M, *Takeuchi K, Watanabe S, Ohno S, Matsuoka R, Kohda D, Nakakita SI, Hiramatsu H, Suzuki Y, Nakayama T, Terada T, Shimizu K, Shimizu N, Shiroishi M, Yanagi Y, *Hashiguchi T. Trisaccharide containing alpha2,3-linked sialic acid is a receptor for mumps virus.
    Proc Natl Acad Sci U S A. 2016;113(41):11579-84.
  19. Fusco ML, Hashiguchi T, Cassan R, Biggins JE, Murin CD, Warfield KL, Li S, Holtsberg FW, Shulenin S, Vu H, Olinger GG, Kim DH, Whaley KJ, Zeitlin L, Ward AB, Nykiforuk C, Aman MJ, Berry JD, *Saphire EO. Protective mAbs and Cross-Reactive mAbs Raised by Immunization with Engineered Marburg Virus GPs.
    PLoS pathogens. 2015;11(6):e1005016. p1-17
  20. Hashiguchi T, Fusco ML, Bornholdt ZA, Lee JE, Flyak AI, Matsuoka R, Kohda D, Yanagi Y, Hammel M, Crowe JE Jr, *Saphire EO. Structural basis for Marburg virus neutralization by a cross-reactive human antibody.
    Cell. 2015;160(5):904-12.
  21. Flyak AI, Ilinykh PA, Murin CD, Garron T, Shen X, Fusco ML, Hashiguchi T, Bornholdt ZA, Slaughter JC, Sapparapu G, Klages C, Ksiazek TG, Ward AB, Saphire EO, Bukreyev A, *Crowe JE Jr. Mechanism of human antibody-mediated neutralization of marburg virus.
    Cell. 2015;160(5):893-903.
  22. Hashiguchi T, Ose T, Kubota M, Maita N, Kamishikiryo J, Maenaka K, *Yanagi Y. Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM.
    Nat Struct Mol Biol. 2011;18(2):135-41.
  23. Hashiguchi T, Kajikawa M, Maita N, Takeda M, Kuroki K, Sasaki K, Kohda D, *Yanagi Y, *Maenaka K. Crystal structure of measles virus hemagglutinin provides insight into effective vaccines.
    Proc Natl Acad Sci U S A. 2007;104(49):19535-40.