Updated on 2024/07/28

Information

 

写真a

 
SHIBATA TOSHIO
 
Organization
Faculty of Science Department of Biology Assistant Professor
School of Sciences Department of Biology(Joint Appointment)
Graduate School of Systems Life Sciences Department of Systems Life Sciences(Joint Appointment)
Title
Assistant Professor
Contact information
メールアドレス
Profile
腸管では、病原細菌に対しては自然免疫による排除を行う一方で、常在細菌に対しては過剰に排除することなく、腸内細菌の恒常性を精緻に制御している。しかしながら、このような免疫寛容系を維持する機構は、哺乳類から無脊椎動物にわたり、依然として未解決の問題である。現在、ショウジョウバエをモデル生物にして、常在細菌との共生を可能にしている分子機構を解析を進めている。 同時に、脂質修飾を介したタンパク質の細胞内輸送や細胞外分泌機構、またタンパク質架橋酵素であるトランスグルタミナーゼの機構解析を、個体~分子レベルで解析を行っている。

Degree

  • Doctor of Philosophy

Research Interests・Research Keywords

  • Research theme:Unconventional protein secretion pathway mediated by fatty acylation

    Keyword:Myristoylation, Palmitoylation, Exosomes

    Research period: 2015.4

  • Research theme:Transglutaminase-catalyzed Crosslinking Suppresses Innate Immune Signaling in the Drosophila Gut

    Keyword:Transglutaminase, Drosophila, IMD pathway

    Research period: 2011.4

Awards

  • 古田優秀論文賞

    2021.9   日本比較免疫学会   Roles of the clip domains of two protease zymogens in the coagulation cascade in horseshoe crabs

  • 日本比較免疫学会優秀論文賞

    2019.9   日本比較免疫学会  

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    リポ多糖依存的なプロテアーゼ前駆体の自己触媒的活性化機構

  • 日本生化学会奨励賞

    2019.9   日本生化学会  

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    キイロショウジョウバエを用いたトランスグルタミナーゼの生理機能と分泌機構の解析

  • 平成29年度日本生化学会九州支部奨励賞

    2017.5   日本生化学会九州支部  

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    キイロショウジョウバエを用いたトランスグルタミナーゼの機能と分泌機構の解明に対する功績

  • Young Research Award

    2015.12  

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    細菌感染時の生体防御タンパク質の分泌機構解明に対する功績

  • 第87回日本生化学会大会若手優秀発表賞

    2014.10   日本生化学会  

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    腸内細菌に対する免疫寛容による腸管恒常性維持機構解明に対する功績

  • 平成26年度日本生体防御学会学術奨励賞

    2014.7   日本生体防御学会  

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    ショウジョウバエの腸内細菌に対する免疫応答と寛容の分子機構解明に対する功績

  • 平成25年度日本比較免疫学会古田奨励賞

    2013.8   日本比較免疫学会  

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    架橋酵素による腸管上皮の情報伝達制御と腸内細菌叢の維持機構解明に対する功績

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Papers

  • Drosophila TG-A transglutaminase is secreted via an unconventional Golgi-independent mechanism involving exosomes and two types of fatty acylations Reviewed International journal

    Toshio Shibata, Jinki Hadano, Daichi Kawasaki, Xiaoqing, Shun-ichiro Kawabata

    The Journal of Biological Chemistry   292 ( 25 )   10723 - 10734   2017.6

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    Language:English   Publishing type:Research paper (scientific journal)  

    Drosophila TG-A transglutaminase is secreted via an unconventional Golgi-independent mechanism involving exosomes and two types of fatty acylations
    Transglutaminases (TGs) play essential intracellular and extracellular roles by covalently cross-linking many proteins. Drosophila TG is encoded by one gene and has two alternative splicing-derived isoforms, TG-A and TG-B, which contain distinct N-terminal 46- and 38-amino acid sequences, respectively. The TGs identified to date do not have a typical endoplasmic reticulum (ER)-signal peptide, and the molecular mechanisms of their secretion under physiologic conditions are unclear. Immunocytochemistry revealed that TG-A localizes to multivesicular-like structures, whereas TG-B localizes to the cytosol. We also found that TG-A, but not TG-B, was modified concomitantly by N-myristoylation and S-palmitoylation, and N-myristoylation was a pre-requisite for S-palmitoylation. Moreover, TG-A, but not TG-B, was secreted in response to calcium signaling induced by Ca2+ ionophores and uracil, a pathogenic bacteria-derived substance. Brefeldin A and monensin, inhibitors of the ER/Golgi-mediated conventional pathway, did not suppress TG-A secretion, whereas inhibition of S-palmitoylation by 2-bromopalmitate blocked TG-A secretion. Ultracentrifugation, electron microscopy analyses, and treatments with inhibitors of multivesicular body formation revealed that TG-A was secreted via exosomes together with co-transfected mammalian CD63, an exosomal marker, and the secreted TG-A was taken up by other cells. The 8-residue N-terminal fragment of TG-A containing the fatty acylation sites was both necessary and sufficient for the exosome-dependent secretion of TG-A. In conclusion, TG-A is secreted through an unconventional ER/Golgi-independent pathway involving two types of fatty acylations and exosomes.

    DOI: 10.1074/jbc.M117.779710

  • Crosslinking of a Peritrophic Matrix Protein Protects Gut Epithelia from Bacterial Exotoxins Reviewed International journal

    Toshio Shibata, Kouki Maki, Jinki Hadano, Takumi Fujikawa, Kazuki Kitazaki, Takumi Koshiba, Shun-ichiro Kawabata

    PLOS Pathogens   11 ( 10 )   e1005244   2015.10

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    Crosslinking of a Peritrophic Matrix Protein Protects Gut Epithelia from Bacterial Exotoxins
    Transglutaminase (TG) catalyzes protein-protein crosslinking, which has important and diverse roles in vertebrates and invertebrates. Here we demonstrate that Drosophila TG crosslinks drosocrystallin, a peritrophic matrix protein, to form a stable fiber structure on the gut peritrophic matrix. RNA interference (RNAi) of the TG gene was highly lethal in flies and induced apoptosis of gut epithelial cells after oral infection with Pseudomonas entomophila. Moreover, AprA, a metalloprotease secreted by P. entomophila, digested non-crosslinked drosocrystallin fibers, but not drosocrystallin fibers crosslinked by TG. In vitro experiments using recombinant drosocrystallin and monalysin proteins demonstrated that monalysin, a pore-forming exotoxin of P. entomophila, was adsorbed on the crosslinked drosocrystallin fibers in the presence of P. entomophila culture supernatant. In addition, gut-specific TG-RNAi flies had a shorter lifespan than control flies after ingesting P. entomophila, whereas the lifespan after ingesting AprA-knockout P. entomophila was at control levels. We conclude that drosocrystallin fibers crosslinked by TG, but not non-crosslinked drosocrystallin fibers, form an important physical barrier against exotoxins of invading pathogenic microbes.

    DOI: 10.1371/journal.ppat.1005244

  • Transglutaminase-Catalyzed Protein-Protein Cross-Linking Suppresses the Activity of the NF-κB–Like Transcription Factor Relish Reviewed International journal

    6 ( 285 )   ra61   2013.7

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1126/scisignal.2003970

  • Effects of Ca2+ ions on the horseshoe crab coagulation cascade triggered by lipopolysaccharide Reviewed

    Keisuke Yamashita, Daisuke Takahashi, Yuki Yamamoto, Shingo Kiyomoto, Toshio Shibata, Shun-ichiro Kawabata

    The Journal of Biochemistry   2023.2

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    Language:English   Publishing type:Research paper (scientific journal)  

    Effects of Ca2+ ions on the horseshoe crab coagulation cascade triggered by lipopolysaccharide
    Abstract

    The lipopolysaccharide (LPS)-triggered horseshoe crab coagulation cascade is composed of three protease zymogens, prochelicerase C (proC), prochelicerase B (proB) and the proclotting enzyme (proCE). In this study, we found that Ca 2+ ions increase the production of the clotting enzyme as a result of a cascade reaction reconstituted by recombinant proteins of wild-type (WT) proC, WT proB and WT proCE. We divided the cascade into three stages: autocatalytic activation of WT proC on the surface of LPS into WT α-chelicerase C (Stage 1); activation of WT proB on the surface of LPS into WT chelicerase B by WT α-chelicerase C (Stage 2) and activation of WT proce into WT CE by chelicerase B (Stage 3). Ca2+ ions enhanced the proteolytic activation in Stage 2, but not those in Stages 1 and 3. Moreover, we performed isothermal titration calorimetry to clarify the interaction of LPS or the recombinant zymogens with Ca2+ ions. LPS interacted with Ca2+ ions at an association constant of Ka = 4.7 × 104 M−1, but not with any of the recombinant zymogens. We concluded that LPS bound with Ca2+ ions facilitates the chain reaction of the cascade as a more efficient scaffold than LPS itself.

    DOI: 10.1093/jb/mvad018

  • A mutant equipped with a regenerated disulfide for the missing his loop of a serine protease zymogen in the horseshoe crab coagulation cascade. Reviewed International journal

    @Keisuke Yamashita, #Naoki Takeshita, #Aina Arita, @Toshio Shibata, @Yuki Kobayashi, @Shun-ichiro Kawabata

    The Journal of Biochemistry   2021.5

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/jb/mvab064

  • ppGpp functions as an alarmone in metazoa. Reviewed International journal

    @Doshun Ito, @Hinata Kawamura, @Akira Oikawa, @Yuta Ihara, @Toshio Shibata, @Nobuhiro Nakamura, @Tsunaki Asano, @Shun-Ichiro Kawabata, @Takashi Suzuki, @Shinji Masuda

    Communications Biology   3 ( 1 )   2020.11

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  • Roles of the clip domains of two protease zymogens in the coagulation cascade in horseshoe crabs. Reviewed International journal

    #Keisuke Yamashita, Toshio Shibata, #Toshiaki Takahashi, @Yuki Kobayashi, Shun-ichiro Kawabata

    Journal of Biological Chemistry   295 ( 26 )   8857 - 8866   2020.6

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1074/jbc.RA119.012452

  • Purification and Assays of Tachylectin-2 Reviewed

    Shun-ichiro Kawabata, Toshio Shibata

    Methods in Molecular Biology   309 - 316   2020.4

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    Purification and Assays of Tachylectin-2

    DOI: 10.1007/978-1-0716-0430-4_30

  • Purification and Assays of Tachylectin-5 Invited Reviewed

    Shun-ichiro Kawabata, Toshio Shibata

    Methods in Molecular Biology   277 - 283   2020.4

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    Language:Others  

    Purification and Assays of Tachylectin-5

    DOI: 10.1007/978-1-0716-0430-4_27

  • Purification and Assays of Tachycitin

    Shun-ichiro Kawabata, Toshio Shibata

    Methods in Molecular Biology   317 - 323   2020.4

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    Language:Others  

    Purification and Assays of Tachycitin

    DOI: 10.1007/978-1-0716-0430-4_31

  • Intermolecular autocatalytic activation of serine protease zymogen factor C through an active transition state responding to lipopolysaccharide Reviewed

    Toshio Shibata, Yuki Kobayashi, Yuto Ikeda, Shun ichiro Kawabata

    Journal of Biological Chemistry   293 ( 29 )   11589 - 11599   2018.7

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    Intermolecular autocatalytic activation of serine protease zymogen factor C through an active transition state responding to lipopolysaccharide
    Horseshoe crab hemolymph coagulation is believed to be triggered by the autocatalytic activation of serine protease zymogen factor C to the active form, -factor C, belonging to the trypsin family, through an active transition state of factor C responding to bacterial lipopolysaccharide (LPS), designated factor C*. However, the existence of factor C* is only speculative, and its proteolytic activity has not been validated. In addition, it remains unclear whether the proteolytic cleavage of the Phe737–Ile738 bond (Phe737 site) of factor C required for the conversion to -factor C occurs intramolecularly or intermolecularly between the factor C molecules. Here we show that the Phe737 site of a catalytic Ser-deficient mutant of factor C is LPS-dependently hydrolyzed by a Phe737 site– uncleavable mutant, clearly indicating the existence of the active transition state of factor C without cleavage of the Phe737 site. Moreover, we found the following facts using several mutants of factor C: the autocatalytic cleavage of factor C occurs intermolecularly between factor C* molecules on the LPS surface; factor C* does not exhibit intrinsic chymotryptic activity against the Phe737 site, but it may recognize a three-dimensional structure around the cleavage site; and LPS is required not only to complete the substrate-binding site and oxyanion hole of factor C* by interacting with the N-terminal region but also to allow the Phe737 site to be cleaved by inducing a conformational change around the Phe737 site or by acting as a scaffold to induce specific protein–protein interactions between factor C* molecules.

    DOI: 10.1074/jbc.RA118.002311

  • Insecticidal activity of the metalloprotease AprA occurs through suppression of host cellular and humoral immunity Reviewed

    Seung Ah Lee, Seong Han Jang, Byung Hyun Kim, Toshio Shibata, Jinwook Yoo, Yunjin Jung, Shun-Ichiro Kawabata, Bok Luel Lee

    Developmental and Comparative Immunology   81   116 - 126   2018.4

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    Insecticidal activity of the metalloprotease AprA occurs through suppression of host cellular and humoral immunity
    The biochemical characterization of virulence factors from entomopathogenic bacteria is important to understand entomopathogen-insect molecular interactions. Pseudomonas entomophila is a typical entomopathogenic bacterium that harbors virulence factors against several insects. However, the molecular actions of these factors against host innate immune responses are not clearly elucidated. In this study, we observed that bean bugs (Riptortus pedestris) that were injected with P. entomophila were highly susceptible to this bacterium. To determine how P. entomophila counteracts the host innate immunity to survive within the insect, we purified a highly enriched protein with potential host insect-killing activity from the culture supernatant of P. entomophila. Then, a 45-kDa protein was purified to homogeneity and identified as AprA which is an alkaline zinc metalloprotease of the genus Pseudomonas by liquid chromatography mass spectrometry (LC-MS). Purified AprA showed a pronounced killing effect against host insects and suppressed both host cellular and humoral innate immunity. Furthermore, to show that AprA is an important insecticidal protein of P. entomophila, we used an aprA-deficient P. entomophila mutant strain (ΔaprA). When ΔaprA mutant cells were injected to host insects, this mutant exhibited extremely attenuated virulence. In addition, the cytotoxicity against host hemocytes and the antimicrobial peptide-degrading ability of the ΔaprA mutant were greatly decreased. These findings suggest that AprA functions as an important insecticidal protein of P. entomophila via suppression of host cellular and humoral innate immune responses.

    DOI: 10.1016/j.dci.2017.11.014

  • Transglutaminase-catalyzed incorporation of polyamines masks the DNA-binding region of the transcription factor Relish Reviewed International journal

    Kouki Maki, Toshio Shibata, Shun-ichiro Kawabata

    The Journal of Biological Chemistry   292 ( 15 )   6369 - 6380   2017.4

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    Transglutaminase-catalyzed incorporation of polyamines masks the DNA-binding region of the transcription factor Relish
    In Drosophila, the final immune deficiency (IMD) pathwaydependent signal is transmitted through proteolytic conversion of the nuclear factor-B (NF-B)-like transcription factor Relish to the active N-Terminal fragment Relish-N. Relish-N is then translocated from the cytosol into the nucleus for the expression of IMD-controlled genes. We previously demonstrated that transglutaminase (TG) suppresses the IMD pathway by polymerizing Relish-N to inhibit its nuclear translocation. Conversely, we also demonstrated that orally ingested synthetic amines, such as monodansylcadaverine (DCA) and biotin-labeled pentylamine, are TG-dependently incorporated into Relish-N, causing the nuclear translocation of modified Relish-N in gut epithelial cells. It remains unclear, however, whether polyamine- containing Relish-N retains transcriptional activity. Here, we used mass spectrometry analysis of a recombinant Relish- N modified with DCA by TG activity after proteolytic digestion and show that the DCA-modified Gln residues are located in the DNA-binding region of Relish-N. TG-catalyzed DCA incorporation inhibited binding of Relish-N to the Rel-responsive element in the NF-B-binding DNA sequence. Subcellular fractionation of TG-expressing Drosophila S2 cells indicated that TG was localized in both the cytosol and nucleus. Of note, natural polyamines, including spermidine and spermine, competitively inhibited TG-dependentDCAincorporation into Relish- N. Moreover, in vivo experiments demonstrated that Relish- N was modified by spermine and that this modification reduced transcription of IMD pathway-controlled cecropin A1 and diptericin genes. These findings suggest that intracellular TG regulates Relish-N-mediated transcriptional activity by incorporating polyamines into Relish-N and via protein-protein cross-linking.

    DOI: 10.1074/jbc.M117.779579

  • RNA Interference Directed against the Transglutaminase Gene Triggers Dysbiosis of Gut Microbiota in Drosophila Reviewed International journal

    Sanae Sekihara, Toshio Shibata, Mai Hyakkendani, Shun-ichiro Kawabata

    The Journal of Biological Chemistry   291 ( 48 )   25077 - 25087   2016.11

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    RNA Interference Directed against the Transglutaminase Gene Triggers Dysbiosis of Gut Microbiota in Drosophila
    We recently reported that transglutaminase (TG) suppresses immune deficiency pathway-controlled antimicrobial peptides (IMD-AMPs), thereby conferring immune tolerance to gut microbes, and that RNAi of the TG gene in flies decreases the lifespan compared with non-TG-RNAi flies. Here, analysis of the bacterial composition of the Drosophila gut by next-generation sequencing revealed that gut microbiota comprising one dominant genus of Acetobacter in non-TG-RNAi flies was shifted to that comprising two dominant genera of Acetobacter and Providencia in TG-RNAi flies. Four bacterial strains, including Acetobacter persici SK1 and Acetobacter indonesiensis SK2, Lactobacillus pentosus SK3, and Providencia rettgeri SK4, were isolated from the midgut of TG-RNAi flies. SK1 exhibited the highest resistance to the IMD-AMPs Cecropin A1 and Diptericin among the isolated bacteria. In contrast, SK4 exhibited considerably lower resistance against Cecropin A1, whereas SK4 exhibited high resistance to hypochlorous acid. The resistance of strains SK1-4 against IMD-AMPs in in vitro assays could not explain the shift of the microbiota in the gut of TG-RNAi flies. The lifespan was reduced in gnotobiotic flies that ingested both SK4 and SK1, concomitant with the production of reactive oxygen species and apoptosis in the midgut, whereas the survival rate was not altered in gnotobiotic flies that monoingested either SK4 or SK1. Interestingly, significant amounts of reactive oxygen species were detected in the midgut of gnotobiotic flies that ingested SK4 and SK2, concomitant with no significant apoptosis in the midgut. In gnotobiotic flies that co-ingested SK4 and SK1, an additional unknown factor(s) may be required to cause midgut apoptosis.

    DOI: 10.1074/jbc.M116.761791

  • Factor B Is the Second Lipopolysaccharide-binding Protease Zymogen in the Horseshoe Crab Coagulation Cascade. Reviewed International journal

    Yuki Kobayashi, Toshiaki Takahashi, Toshio Shibata, Shunsuke Ikeda, Takumi Koshiba, Hikaru Mizumura, Toshio Oda, Shun-ichiro Kawabata

    The Journal of Biological Chemistry   290 ( 31 )   19379 - 19386   2015.6

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    Factor B Is the Second Lipopolysaccharide-binding Protease Zymogen in the Horseshoe Crab Coagulation Cascade.
    Factor B is a serine-protease zymogen in the horseshoe crab coagulation cascade, and it is the primary substrate for activated factor C, the LPS-responsive initiator of the cascade. Factor C is autocatalytically activated to alpha-factor C on LPS and is artificially converted to beta-factor C, another activated form, by chymotrypsin. It is not known, however, whether LPS is required for the activation of factor B. Here we found that wild-type factor B expressed in HEK293S cells is activated by alpha-factor C, but not by beta-factor C, in an LPS-dependent manner and that beta-factor C loses the LPS binding activity of factor C through additional cleavage by chymotrypsin within the N-terminal LPS-binding region. Surface plasmon resonance and quartz crystal microbalance analyses revealed that wild-type factor B binds to LPS with high affinity comparable with that of factor C, demonstrating that factor B is the second LPS-binding zymogen in the cascade. An LPS-binding site of wild-type factor B was found in the N-terminal clip domain, and the activation rate of a clip domain deletion mutant was considerably slower than that of wild-type factor B. Moreover, in the presence of LPS, Triton X-100 inhibited the activation of wild-type factor B by alpha-factor C. We conclude that the clip domain of factor B has an important role in localizing factor B to the surface of Gram-negative bacteria or LPS released from bacteria to initiate effective proteolytic activation by alpha-factor C.

    DOI: 10.1074/jbc.M115.653196

  • The N-terminal Arg Residue Is Essential for Autocatalytic Activation of a Lipopolysaccharide-responsive Protease Zymogen Reviewed International journal

    Yuki Kobayashi, Takafumi Shiga, Toshio Shibata, Miyuki Sako, Katsumi Maenaka, Takumi Koshiba, Hikaru Mizumura, Toshio Oda, Shun-ichiro Kawabata

    The Journal of Biological Chemistry   289 ( 37 )   25987 - 25995   2014.9

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    The N-terminal Arg Residue Is Essential for Autocatalytic Activation of a Lipopolysaccharide-responsive Protease Zymogen
    Factor C, a serine protease zymogen involved in innate immune responses in horseshoe crabs, is known to be autocatalytically activated on the surface of bacterial lipopolysaccharides, but the molecular mechanism of this activation remains unknown. In this study, we show that wild-type factor C expressed in HEK293S cells exhibits a lipopolysaccharide-induced activity equivalent to that of native factor C. Analysis of the N-terminal addition, deletion, or substitution mutants shows that the N-terminal Arg residue and the distance between the N terminus and the tripartite of lipopolysaccharide-binding site are essential factors for autocatalytic activation, and that the positive charge of the N terminus may interact with an acidic amino acid(s) of the molecule to convert the zymogen into an active form. Chemical cross-linking experiments indicate that the N terminus is required to form a complex of the factor C molecules in a sufficiently close vicinity to be chemically cross-linked on the surface of lipopolysaccharides. We propose a molecular mechanism of the autocatalytic activation of the protease zymogen on lipopolysaccharides functioning as a platform to induce specific protein-protein interaction between the factor C molecules.

    DOI: 10.1074/jbc.M114.586933

  • Microbe-Specific C3b Deposition in the Horseshoe Crab Complement System in a C2/Factor B-Dependent or -Independent Manner Reviewed

    Keisuke Tagawa, Toyoki Yoshihara, Toshio Shibata, Kazuki Kitazaki, Yuichi Endo, Teizo Fujita, Takumi Koshiba, Shun-ichiro Kawabata

    PLoS ONE   7 ( 5 )   e36783 - e36783   2012.5

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    Microbe-Specific C3b Deposition in the Horseshoe Crab Complement System in a C2/Factor B-Dependent or -Independent Manner

    DOI: 10.1371/journal.pone.0036783

  • Protein Crosslinking by Transglutaminase Controls Cuticle Morphogenesis in Drosophila Reviewed

    Toshio Shibata, Shigeru Ariki, Naoaki Shinzawa, Ryuta Miyaji, Haruka Suyama, Miyuki Sako, Nobuyuki Inomata, Takumi Koshiba, Hirotaka Kanuka, Shun-ichiro Kawabata

    PLoS ONE   5 ( 10 )   e13477 - e13477   2010.10

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    Protein Crosslinking by Transglutaminase Controls Cuticle Morphogenesis in Drosophila

    DOI: 10.1371/journal.pone.0013477

  • Factor G Utilizes a Carbohydrate-Binding Cleft That Is Conserved between Horseshoe Crab and Bacteria for the Recognition of β-1,3-<scp>d</scp>-Glucans Reviewed

    183 ( 6 )   3810 - 3818   2009.9

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    Language:Others   Publishing type:Research paper (scientific journal)  

    DOI: 10.4049/jimmunol.0900430

  • Factor C Acts as a Lipopolysaccharide-Responsive C3 Convertase in Horseshoe Crab Complement Activation Reviewed

    Shigeru Ariki, Shusaku Takahara, Toshio Shibata, Takaaki Fukuoka, Aya Ozaki, Yuichi Endo, Teizo Fujita, Takumi Koshiba, Shun-ichiro Kawabata

    The Journal of Immunology   181 ( 11 )   7994 - 8001   2008.12

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    Factor C Acts as a Lipopolysaccharide-Responsive C3 Convertase in Horseshoe Crab Complement Activation
    Abstract

    The complement system in vertebrates plays an important role in host defense against and clearance of invading microbes, in which complement component C3 plays an essential role in the opsonization of pathogens, whereas the molecular mechanism underlying C3 activation in invertebrates remains unknown. In an effort to understand the molecular activation mechanism of invertebrate C3, we isolated and characterized an ortholog of C3 (designated TtC3) from the horseshoe crab Tachypleus tridentatus. Flow cytometric analysis using an Ab against TtC3 revealed that the horseshoe crab complement system opsonizes both Gram-negative and Gram-positive bacteria. Evaluation of the ability of various pathogen-associated molecular patterns to promote the proteolytic conversion of TtC3 to TtC3b in hemocyanin-depleted plasma indicated that LPS, but not zymosan, peptidoglycan, or laminarin, strongly induces this conversion, highlighting the selective response of the complement system to LPS stimulation. Although originally characterized as an LPS-sensitive initiator of hemolymph coagulation stored within hemocytes, we identified factor C in hemolymph plasma. An anti-factor C Ab inhibited various LPS-induced phenomena, including plasma amidase activity, the proteolytic activation of TtC3, and the deposition of TtC3b on the surface of Gram-negative bacteria. Moreover, activated factor C present on the surface of Gram-negative bacteria directly catalyzed the proteolytic conversion of the purified TtC3, thereby promoting TtC3b deposition. We conclude that factor C acts as an LPS-responsive C3 convertase on the surface of invading Gram-negative bacteria in the initial phase of horseshoe crab complement activation.

    DOI: 10.4049/jimmunol.181.11.7994

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Books

  • Transglutaminases-Multiple Functional Modifiers and Targets for New Drug Discovery

    ( Role: Joint author)

    2015.12 

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    Language:English   Book type:Scholarly book

    The existing knowledge of invertebrate transglutaminases with an emphasis on the importance of various physiological properties in innate immune reactions.

  • 動物の事典

    @川畑 俊一郎、@柴田 俊生( Role: Joint author)

    朝倉書店  2020.11 

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    Responsible for pages:第10章「動物の免疫」担当   Language:Japanese   Book type:Scholarly book

  • 研究者が教える動物飼育 第1巻―ゾウリムシ,ヒドラ,貝,エビなど―

    柴田 俊生, 川畑 俊一郎( Role: Joint author)

    共立出版  2012.5 

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    Language:Japanese   Book type:General book, introductory book for general audience

Presentations

  • 脂質修飾を介したショウジョウバエトランスグルタミナーゼおよび自然免疫の機能制 Invited

    @柴田 俊生

    日本生化学会  2023.10 

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    Event date: 2023.10

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Venue:福岡県   Country:Japan  

  • キイロショウジョウバエを用いたトランスグルタミナーゼの生理機能と分泌機構の解析

    柴田俊生

    日本生化学会大会(奨励賞受賞講演)  2019.9 

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    Event date: 2019.9

    Language:Japanese  

    Venue:横浜市   Country:Japan  

  • ショウジョウバエの腸内細菌に対する免疫応答と寛容の分子機構 Invited

    柴田 俊生

    第36回日本炎症・再生医学会  2015.7 

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    Event date: 2015.7

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Country:Japan  

  • Transglutaminase-Catalyzed Protein-Protein Crosslinking Maintains the Gut Epithelial Immunity in Drosophila Invited International conference

    The 55th Annual Drosophila Research Conference  2014.3 

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    Event date: 2014.3

    Language:English   Presentation type:Symposium, workshop panel (public)  

    Country:United States  

  • キイロショウジョウバエトランスグルタミナーゼの架橋反応による腸管免疫の維持機構 Invited

    柴田 俊生, 関原早苗, 藤川匠, 宮地隆太, 石原 健, 小柴 琢己, 川畑 俊一郎

    第85回日本生化学会  2012.12 

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    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Venue:福岡   Country:Japan  

  • ショウジョウバエ自然免疫の応答制御と腸内細菌の共生成立の分子機構 Invited

    柴田 俊生

    平成26年度日本生化学会九州支部例会  2014.5 

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    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Venue:福岡市   Country:Japan  

  • ショウジョウバエの腸内細菌に対する免疫応答と寛容の分子機構

    柴田 俊生

    第25回日本生体防御学会学術総会・日本比較免疫学会第26回学術集会合同学会(日本生体防御学会学術奨励賞受賞講演)  2014.7 

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    Language:Japanese  

    Venue:仙台市   Country:Japan  

  • 腸内細菌に対する免疫寛容による腸管恒常性維持

    柴田 俊生

    第87回日本生化学会大会  2014.10 

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    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:京都市   Country:Japan  

  • タンパク質の N-ミリストイル化を介したショウジョウバエ自然免疫経路の制御機構解析

    @柴田 俊生

    日本生体防御学会  2023.9 

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    Event date: 2023.9

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:京都府   Country:Japan  

  • ショウジョウバエトランスグルタミナーゼによる宿主腸管免疫と細菌叢の維持

    柴田俊生

    日本生化学会大会(シンポジウム「タンパク質を架橋接着させる酵素・トランスグルタミナーゼが担う生体機能構築」)  2022.11 

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    Event date: 2022.11

    Language:Others  

    Country:Other  

  • リポ多糖依存的なプロテアーゼ前駆体の自己触媒的活性化機構

    柴田俊生

    日本比較免疫学会学術集会(古田優秀論文賞受賞講演)  2019.9 

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    Event date: 2019.9

    Language:Japanese  

    Venue:福岡県   Country:Japan  

  • Functional analysis on the Drosophila peritrophic matrix protein International conference

    @Toshio Shibata

    Asian Invertebrate Immunity Symposium  2018.9 

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    Event date: 2018.9

    Language:English   Presentation type:Oral presentation (general)  

    Country:Japan  

  • ショウジョウバエ囲食膜タンパク質の機能解析

    柴田俊生

    日本生化学会九州支部例会  2018.6 

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    Event date: 2018.6 - 2018.7

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:福岡市   Country:Japan  

  • Drosophila transglutaminase is secreted via an unconventional pathway involving exosomes and two types of fatty acylations International conference

    Toshio Shibata

    Goadon Research Conference  2018.6 

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    Event date: 2018.6

    Language:Japanese  

    Country:Switzerland  

  • ショウジョウバエ腸管のムチン様タンパク質の機能解析

    柴田俊生

    日本生体防御学会学術総会  2018.6 

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    Event date: 2018.6

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:京都市   Country:Japan  

  • キイロショウジョウバエにおけるトランスグルタミナーゼの機能と分泌機構 Invited

    柴田俊生

    2017年度生命科学系学会合同年次大会  2017.12 

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    Event date: 2017.12

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Venue:神戸市   Country:Japan  

  • Transglutaminase-catalyzed crosslinking of peritrophic matrix proteins maintains the gut epithelial immunity in Drosophila Invited International conference

    Toshio Shibata

    Entomology 2017  2017.11 

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    Event date: 2017.11

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Country:United States  

  • Transglutaminase-catalyzed crosslinking of peritrophic matrix proteins maintains the gut epithelial immunity in Drosophila International conference

    Toshio Shibata

    European Drosophila Research Conference  2017.9 

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    Event date: 2017.9

    Language:English   Presentation type:Oral presentation (general)  

    Country:United Kingdom  

  • 脂質修飾とエクソソームを介したショウジョウバエトランスグルタミナーゼの分泌機構

    柴田俊生

    日本比較免疫学会  2017.8 

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    Event date: 2017.8

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • エクソソームを介したショウジョウバエトランスグルタミナーゼの細胞外分泌機構

    柴田俊生

    日本生体防御学会  2017.7 

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    Event date: 2017.7

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:相模原市   Country:Japan  

  • エクソソームを介したショウジョウバエトランスグルタミナーゼの細胞外分泌機構

    柴田俊生

    日本生化学会九州支部例会  2017.5 

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    Event date: 2017.5

    Language:Japanese  

    Venue:宮崎県   Country:Japan  

  • ショウジョウバエトランスグルタミナーゼの細胞外分泌機構解明

    柴田 俊生

    平成28年度日本生化学会九州支部例会  2016.5 

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    Event date: 2016.5

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:鹿児島県   Country:Japan  

  • 脂質修飾が引き起こすショウジョウバエトランスグルタミナーゼの細胞内局在性の変化

    柴田 俊生

    第18回トランスグルタミナーゼ研究会学術集会  2015.12 

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    Event date: 2015.12

    Language:Japanese  

    Country:Japan  

  • 脂質修飾が引き起こすショウジョウバエトランスグルタミナーゼの細胞内局在性の変化

    柴田 俊生

    2015.12 

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    Event date: 2015.12

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:兵庫県   Country:Japan  

  • 脂質修飾が引き起こす架橋酵素の細胞内局在性の変化

    柴田 俊生

    日本比較免疫学会第27回学術集会  2015.8 

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    Event date: 2015.8

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:福井県   Country:Japan  

  • 脂質修飾によるトランスグルタミナーゼの局在化の制御機構

    柴田 俊生

    第26回日本生体防御学会学術総会  2015.7 

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    Event date: 2015.7

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:東京都   Country:Japan  

  • 腸内細菌に対する免疫寛容による腸管恒常性維持

    柴田 俊生

    第17回トランスグルタミナーゼ研究会学術集会  2014.10 

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    Event date: 2014.10

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • タンパク質架橋による自然免疫の応答制御と腸内細菌共生成立の分子機構

    柴田 俊生

    第38回蛋白質と酵素の構造と機能に関する九州シンポジウム  2014.9 

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    Event date: 2014.9

    Language:Japanese  

    Country:Japan  

  • Transglutaminase-catalyzed Crosslinking Suppresses the Activity of the NF-kB-like Transcription Factor Relish in Drosophila Invited

    The 1st Asian Invertebrate Immunology Symposium  2014.2 

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    Event date: 2014.2

    Language:English   Presentation type:Symposium, workshop panel (public)  

    Country:Korea, Republic of  

  • Transglutaminase-Catalyzed Protein-Protein Crosslinking Suppresses the Activity of the NF-kB-Like Transcription Factor Relish International conference

    Keystone Symposia on Molecular and Cellular Biology  2014.1 

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    Event date: 2014.1

    Language:Japanese  

    Country:United States  

  • キイロショウジョウバエ腸管の囲食膜タンパク質架橋化による生体防御機構

    柴田 俊生

    第86回日本生化学会大会  2013.9 

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    Event date: 2013.9

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • キイロショウジョウバエ腸管の囲食膜タンパク質架橋化による生体防御機構

    柴田 俊生

    第16回トランスグルタミナーゼ研究会&日本ポリアミン学会合同学術集会  2013.9 

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    Event date: 2013.9

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • 架橋酵素による腸管上皮の情報伝達制御と腸内細菌叢の維持機構

    柴田 俊生

    日本比較免疫第25回学術集会  2013.8 

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    Event date: 2013.8

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • 架橋酵素による腸管上皮の情報伝達制御と腸内細菌叢の維持機構

    柴田 俊生

    第24回日本生体防御学会  2013.7 

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    Event date: 2013.7

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Country:Japan  

  • ハエ腸管の囲食膜タンパク質ドロソクリスタリン架橋化と生体防御機構の解明

    柴田 俊生

    平成25年度日本生化学会九州支部例会  2013.5 

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    Event date: 2013.5

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • キイロショウジョウバエトランスグルタミナーゼの架橋反応による腸管免疫の維持機構

    柴田 俊生

    第15回トランスグルタミナーゼ研究会学術集会  2012.12 

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    Event date: 2012.12

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • Transglutaminase-catalyzed protein-protein crosslinking of Relish suppresses innate immune signaling in Drosophila International conference

    Homeostatic Inflammation Symposium  2012.10 

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    Event date: 2012.10

    Language:English  

    Country:Japan  

  • Transglutaminase-catalyzed Relish Crosslinking Suppresses Innate Immune Signaling in the Drosophila Gut International conference

    International Society of Developmental and Comparative Immunology  2012.7 

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    Event date: 2012.7

    Language:English   Presentation type:Oral presentation (general)  

    Country:Japan  

  • キイロショウジョウバエトランスグルタミナーゼの架橋反応による腸管免疫の維持機構

    柴田 俊生

    平成24年度日本生化学会九州支部例会  2012.5 

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    Event date: 2012.5

    Language:Japanese   Presentation type:Oral presentation (general)  

    Country:Japan  

  • Transglutaminase-Catalyzed Protein-Protein Crosslinking Maintains the Gut Epithelial Immunity International conference

    Gordon Research Conference, Transglutaminases in Human Disease Processes  2014.7 

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    Language:English  

    Country:Italy  

  • 脂質修飾によるトランスグルタミナーゼの分泌機構

    柴田俊生

    日本生体防御学会学術総会(若手シンポジウム)  2016.9 

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    Language:Others  

    Country:Other  

  • 感染防御に関わるショウジョウバエトランスグルタミナーゼの細胞外分泌経路の解析

    柴田俊生

    日本生化学会大会  2016.9 

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    Language:Others  

    Country:Other  

  • Fatty-acid modifications control intracellular localization and secretion of Drosophila transglutaminase

    Toshio Shibata

    Asian Invertebrate Immunity Symposium 2016  2016.10 

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    Language:Others  

    Country:Other  

  • ショウジョウバエの免疫寛容を介した腸管恒常性維持の分子機構 Invited

    柴田俊生

    日本分子生物学会年会(シンポジウム「宿主ーマイクロバイオータ相互作用」)  2016.12 

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    Language:Others  

    Country:Other  

  • Drosophila Transglutaminase-A is secreted via an unconventional pathway involving two types of fatty acylations and exosomes

    Toshio Shibata

    BIT's 8th Annual Congress of Molecular & Cell Biology  2018.10 

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    Language:English  

    Country:Other  

  • キイロショウジョウバエを用いたトランスグルタミナーゼの生理機能と分泌機構の解析

    柴田俊生

    日本生化学会大会(シンポジウム「タンパク質架橋化反応から展開する医療と創薬へ向けた基礎研究」)  2020.9 

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    Language:Others  

    Country:Other  

  • ショウジョウバエのフィブリノーゲン様レクチンの機能解析

    柴田俊生, 小城真菜, 鳴海佳輔, 川畑俊一郎

    日本生化学会九州支部例会  2022.6 

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    Country:Other  

  • ショウジョウバエ腸管における宿主免疫系ー細菌叢の相互作用 Invited

    柴田俊生

    日本生体防御学会学術総会(シンポジウム「系統進化から読み解く自己・非自己認識系の普遍性と多様性」)  2022.9 

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    Language:Others  

    Country:Other  

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MISC

  • Pluripotency and a secretion mechanism of Drosophila Transglutaminase

    Toshio Shibata, Shun-ichiro Kawabata

    2018.3

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    Language:Japanese  

    Pluripotency and a secretion mechanism of Drosophila transglutaminase
    Transglutaminase (TG) catalyses the formation of an isopeptide bond between glutamine and lysine residues and amine incorporation into specific glutamine residues. TG is conserved in all metazoans and functions both intracellularly and extracellularly. Here we review the existing knowledge of Drosophila TG with an emphasis on its pluripotency: Drosophila TG (i) plays a key role in cuticular morphogenesis, haemolymph coagulation, and entrapment against invading pathogens, (ii) suppresses the immune deficiency pathway to enable immune tolerance against commensal bacteria through the incorporation of polyamines into the nuclear factor-iB-like transcription factor Relish as well as through the protein-protein cross-linking of Relish, (iii) forms a physical matrix in the gut through cross-linking of chitin-binding proteins and (iv) is involved in the maintenance of homeostasis in microbiota in the gut. Moreover, we review the evidence that TG-A, one of alternative splicing-derived isoforms of Drosophila TG, is secreted through an endoplasmic reticulum/Golgi-independent pathway involving exosomes and fatty acylations.

    DOI: 10.1093/jb/mvx059

  • New insights into the hemolymph coagulation cascade of horseshoe crabs initiated by autocatalytic activation of a lipopolysaccharide-sensitive zymogen Reviewed

    @Shun-ichiro Kawabata, @Toshio Shibata

    Developmental and Comparative Immunology   2022.10

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

    DOI: 10.1016/j.dci.2022.104491

  • リポ多糖を介したプロテアーゼ前駆体の自己触媒的活性化機構 Reviewed

    @川畑俊一郎,@柴田俊生

    生化学   2022.2

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

    DOI: 10.14952/SEIKAGAKU.2022.940037

  • カブトガニの病原体に対する自然免疫の応答と制御

    柴田 俊生, 川畑 俊一郎

    化学と生物   2012.4

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    Language:Japanese  

    DOI: 10.1271/kagakutoseibutsu.50.277

  • The lipopolysaccharide-activated innate immune response network of the horseshoe crab

    Shun-ichiro Kawabata, Takumi Koshiba, Toshio Shibata

    Invertebrate Survival Journal   2009.5

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    Language:English   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)  

Professional Memberships

  • 日本生化学会

  • 日本生体防御学会

  • 日本比較免疫学会

Academic Activities

  • 座長

    日本生化学会九州支部例会  ( Web開催 ) 2022.6

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    Type:Competition, symposium, etc. 

  • Microbiology and Immunology International contribution

    2022.4 - 2023.3

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    Type:Academic society, research group, etc. 

  • Screening of academic papers

    Role(s): Peer review

    2022

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:6

  • Screening of academic papers

    Role(s): Peer review

    2021

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:7

  • Screening of academic papers

    Role(s): Peer review

    2020

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:4

  • 企画立案・運営等

    ( 九州大学 Japan ) 2019.9

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    Type:Competition, symposium, etc. 

  • Screening of academic papers

    Role(s): Peer review

    2019

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:4

  • Planning, management, etc.

    Asian Invertebrate Immunity Symposium 2018  ( Japan ) 2018.9

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    Type:Competition, symposium, etc. 

  • 学会オーガナイザー International contribution

    2018.9

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    Type:Competition, symposium, etc. 

  • パネル司会・セッションチェア等

    日本比較免疫学会第29回学術集会  2018.8

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    Type:Competition, symposium, etc. 

  • Screening of academic papers

    Role(s): Peer review

    2018

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:1

  • Screening of academic papers

    Role(s): Peer review

    2017

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:6

  • パネル司会・セッションチェア等

    日本比較免疫学会第27回学術集会  2016.8

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    Type:Competition, symposium, etc. 

  • パネル司会・セッションチェア等

    平成28年度日本生化学会九州支部例会  2016.5

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    Type:Competition, symposium, etc. 

  • Screening of academic papers

    Role(s): Peer review

    2016

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:4

  • パネル司会・セッションチェア等

    平成27年度日本生化学会九州支部例会  ( 福岡市 Japan ) 2015.5

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    Type:Competition, symposium, etc. 

    Number of participants:200

  • 企画立案・運営等, 査読

    平成27年度日本生化学会九州支部例会  2015.5

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    Type:Competition, symposium, etc. 

  • パネル司会・セッションチェア等

    第25回日本生体防御学会学術総会・日本比較免疫学会第26回学術集会合同学会  ( 仙台市 Japan ) 2014.7

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    Type:Competition, symposium, etc. 

  • 座長(Chairmanship)

    平成26年度日本生化学会九州支部例会  ( 福岡市 ) 2014.5

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    Type:Competition, symposium, etc. 

  • 企画立案・運営等, パネル司会・セッションチェア等

    平成26年度日本生化学会九州支部例会  ( 福岡市 Japan ) 2014.5

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    Type:Competition, symposium, etc. 

    Number of participants:180

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Research Projects

  • 乳素材・乳酸菌が腸内免疫機能に及ぼす影響とその機構の解明

    2023.4 - 2025.3

    共同研究

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    Authorship:Principal investigator  Grant type:Other funds from industry-academia collaboration

  • 細胞外小胞への選択的・効率的なタンパク質輸送系構築

    Grant number:21K05385  2021 - 2023

    日本学術振興会  科学研究費助成事業  基盤研究(C)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 脂質修飾によるトランスグルタミナーゼの exosome 依存的な分泌機構解明

    Grant number:17K15121  2017 - 2019

    科学研究費助成事業  若手研究(B)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 架橋酵素による自然免疫の応答制御と腸内細菌の維持機構

    Grant number:15H04353  2015 - 2017

    日本学術振興会  科学研究費助成事業  基盤研究(C)

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    Grant type:Scientific research funding

  • 脂質修飾による免疫反応調節機構の解明

    2014 - 2017

    九州大学教育研究プログラム・研究拠点形成プロジェクト TTタイプ

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    Authorship:Principal investigator  Grant type:On-campus funds, funds, etc.

  • 免疫制御による多臓器恒常性維持機構解明

    Grant number:26860333  2014 - 2015

    科学研究費助成事業  若手研究(B)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 腸管における架橋酵素を介したシグナル伝達制御と腸内細菌との共生成立の分子機構

    Grant number:24570164  2012 - 2014

    日本学術振興会  科学研究費助成事業  基盤研究(C)

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    Grant type:Scientific research funding

  • 腸管における自然免疫経路の制御機構と腸内細菌恒常性維持の分子機構解明

    2012

    九州大学教育研究プログラム・研究拠点形成プロジェクト(D-3タイプ)

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    Authorship:Principal investigator  Grant type:On-campus funds, funds, etc.

  • タンパク質架橋反応による腸管免疫の情報伝達制御

    Grant number:23890147  2011 - 2012

    日本学術振興会  科学研究費助成事業  研究活動スタート支援

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    Authorship:Principal investigator  Grant type:Scientific research funding

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Class subject

  • 応用生物化学実験

    2024.4 - 2024.9   First semester

  • 生物学演習I

    2023.10 - 2024.3   Second semester

  • 自然科学総合実験

    2023.10 - 2023.12   Fall quarter

  • 応用生物化学実験

    2023.4 - 2023.9   First semester

  • 自然科学総合実験

    2022.12 - 2023.2   Winter quarter

  • 生物学演習I

    2022.10 - 2023.3   Second semester

  • 応用生物化学実験

    2022.4 - 2022.9   First semester

  • 自然科学総合実験

    2021.12 - 2022.2   Winter quarter

  • 生物学演習I

    2021.10 - 2022.3   Second semester

  • 応用生物科学実験

    2021.4 - 2021.9   First semester

  • 自然科学総合実験

    2020.10 - 2021.3   Second semester

  • 生物学演習I

    2020.10 - 2021.3   Second semester

  • 応用生物化学実験

    2020.10 - 2020.12   Fall quarter

  • 自然科学総合実験

    2019.10 - 2019.12   Fall quarter

  • 生物学演習I

    2019.4 - 2019.9   First semester

  • 応用生物化学実験

    2019.4 - 2019.9   First semester

  • 自然科学総合実験

    2018.12 - 2019.2   Winter quarter

  • 応用生物化学実験

    2018.4 - 2018.6   Spring quarter

  • 自然科学総合実験

    2017.10 - 2017.12   Fall quarter

  • 応用生物化学実験

    2017.4 - 2017.6   Spring quarter

  • 自然科学総合実験

    2016.10 - 2017.3   Second semester

  • 応用生物化学実験

    2016.4 - 2016.9   First semester

  • 自然科学総合実験

    2015.10 - 2016.3   Second semester

  • 応用生物化学実験

    2015.4 - 2015.9   First semester

  • 自然科学総合実験

    2014.10 - 2015.3   Second semester

  • 応用生物化学実験

    2014.4 - 2014.9   First semester

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Social Activities

  • 高校生物研究部支援

    修猷館高等学校  2023.5

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    Audience: General, Scientific, Company, Civic organization, Governmental agency

  • ジョイントセミナー(出張講座)

    佐賀県立鹿島高等学校  2019.8

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    Audience: General, Scientific, Company, Civic organization, Governmental agency

  • ジョイントセミナー(出張講座)

    佐賀県立鹿島高校  2019.8

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    Audience: Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

  • 平成25年度九州大学理学部先端自然科学講演会・平成25年度福岡県高等学校理科部会 第1回研修会

    2013.8

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    Audience: Infants, Schoolchildren, Junior students, High school students

    Type:Seminar, workshop

Media Coverage

  • 九大、ハエの架橋酵素が脂質修飾とエクソソームを介して分泌されることが判明

    日本経済新聞  2017.5

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    九大、ハエの架橋酵素が脂質修飾とエクソソームを介して分泌されることが判明

  • 九大、架橋(糊付け)酵素とポリアミンによる免疫過剰反応の抑制機構の解明

    日本経済新聞  2017.3

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    九大、架橋(糊付け)酵素とポリアミンによる免疫過剰反応の抑制機構の解明

Travel Abroad

  • 2008.12 - 2009.2

    Staying countory name 1:Sweden   Staying institution name 1:Uppsala University

    Staying countory name 2:Sweden   Staying institution name 2:Stockholm University