九州大学 研究者情報
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基本情報 研究活動 教育活動 社会活動
李 在萬(りー じやえまん) データ更新日:2019.06.12

准教授 /  農学研究院 資源生物科学部門 農業生物資源学講座


主な研究テーマ
昆虫工場におけるタンパク質糖鎖修飾の解析と改変
キーワード:糖鎖修飾 バキュロウイルス発現系 N型糖鎖 O型糖鎖
2015.04.
バキュロウイルスを利用した高効率組換えタンパク質生産に関する研究
キーワード:カイコ、バキュロウイルス、組換えタンパク質
2004.10.
鱗翅目昆虫における遺伝子機能解析汎用ベクタ−系の開発と遺伝子組換え昆虫への応用
キーワード:カイコ、汎用ベクタ−系、有用プロモーター
2000.10.
研究業績
主要原著論文
1. Yurie Kinoshita, Jian Xu, Akitsu Masuda, Kosuke Minamihata, Noriho Kamiya, Hiroaki Mon, Ryosuke Fujita, Takahiro Kusakabe, Man Lee, Expression and purification of biologically active human granulocyte-macrophage colony stimulating factor (hGM-CSF) using silkworm-baculovirus expression vector system, Protein Expression and Purification, 10.1016/j.pep.2019.03.010, 159, 69-74, 2019.07, [URL], Human granulocyte-macrophage colony stimulating factor (hGM-CSF) is a hematopoietic growth factor. It is widely employed as a therapeutic agent targeting neutropenia in cancer patients undergoing chemotherapy and in patients with AIDS or after bone marrow transplantation. In this study, we constructed the recombinant baculoviruses for the expression of recombinant hGM-CSF (rhGM-CSF) with two small affinity tags (His-tag and Strep-tag) at the N or C-terminus. Compared to N-tagged rhGM-CSF, C-tagged rhGM-CSF was highly recovered from silkworm hemolymph. The purified rhGM-CSF proteins migrated as a diffuse band and were confirmed to hold N-glycosylations. A comparable activity was achieved when commercial hGM-CSF was tested as a control. Considering the high price of hGM-CSF in the market, our results and strategies using silkworm-baculovirus system can become a great reference for mass production of the active rhGM-CSF at a lower cost..
2. Takumi Yano, Man Lee, Jian Xu, Yoshiki Morifuji, Akitsu Masuda, Masato Hino, Daisuke Morokuma, Ryosuke Fujita, Masateru Takahashi, Takahiro Kusakabe, Hiroaki Mon, Expression of the thermostable Moloney murine leukemia virus reverse transcriptase by silkworm-baculovirus expression system, Journal of Asia-Pacific Entomology, 10.1016/j.aspen.2019.02.008, 22, 2, 453-457, 2019.06, [URL], Reverse transcriptase from Moloney murine leukemia virus (MMLVRT) is an RNA dependent DNA polymerase, which has been used as a fundamental tool for molecular biology and biotechnology. The secondary structures formed in the RNA templates decrease the accessibility of the reverse transcriptase to the RNA templates; it is important to unfold the RNA secondary structure by increasing the reaction temperature to perform the successful transcription. In this study, we applied silkworm baculovirus expression vector system (silkworm-BEVS) to mass-produce and purify the recombinant MMLVRTs with the N- or C- terminal tandem tags. We confirmed that both of the recombinant MMLVRT enzymes have intact DNA polymerase activity. It is notable that C- terminal tagged MMLVRT outperformed MMLVRT obtained from the E. coli expression system in terms of thermostability and sensitivity to low quantities of RNA template. Taken together, these results demonstrate that silkworm-BEVS is a promising alternative strategy to produce the functional and thermostable reverse transcriptase..
3. Akihiro Morio, Jian Xu, Akitsu Masuda, Yurie Kinoshita, Masato Hino, Daisuke Morokuma, Hatsumi M. Goda, Nozomu Okino, Makoto Ito, Hiroaki Mon, Ryosuke Fujita, Takahiro Kusakabe, Man Lee, Expression, purification, and characterization of highly active endo-α-N-acetylgalactosaminidases expressed by silkworm-baculovirus expression system, Journal of Asia-Pacific Entomology, 10.1016/j.aspen.2019.01.009, 22, 2, 404-408, 2019.06, [URL], The O-glycosidase, endo-α-N-acetylgalactosaminidase from Enterococcus faecalis (endoEF) catalyzes the cleavage of core 1 and core 3 type O-linked disaccharides between GalNAc and serine or threonine residues from glycoproteins. The endoEF has broad substrate specificity and thus is extensively utilized for the structural and functional analysis of the O-linked glycans. In this study, we expressed and purified the recombinant endoEF (rEndoEF) by using the silkworm-baculovirus expression vector system (Silkworm-BEVS) and confirmed the deglycosylation activity of rEndoEF targeting reporter glycoproteins, which was equivalent to the commercial O-glycosidase. Thus, our study provides important clues to produce highly active rEndoEF O-glycosidases employing silkworm-BEVS as an alternative..
4. Patmawati, Kosuke Minamihata, Tsuneyuki Tatsuke, Man Lee, Takahiro Kusakabe, Noriho Kamiya, Functional horseradish peroxidase−streptavidin chimeric proteins prepared using a silkworm-baculovirus expression system for diagnostic purposes, Journal of Biotechnology, 10.1016/j.jbiotec.2019.03.007, 297, 28-31, 2019.05, [URL], Rapid, convenient, sensitive detection methods are of the utmost importance in analytical tools. Enzyme-based signal amplification using horseradish peroxidase (HRP) is commonly implemented in clinical diagnostics kits based on enzyme-linked immunosorbent assay (ELISA), by which the limit of detection is greatly improved. Herein we report the design and preparation of recombinant fusion proteins comprising HRP and streptavidin (Stav), in which HRP was fused to either the N- or C-terminus of Stav ((HRP)
4
–Stav or Stav–(HRP)
4
, respectively) using a baculovirus-silkworm expression system. Both (HRP)
4
–Stav and Stav–(HRP)
4
were secreted in the apo form but they were easily converted to the holo form and activated by simple incubation with hemin overnight at 4 °C. The activated (HRP)
4
–Stav and Stav–(HRP)
4
could be combined with a commercial biotinylated anti-OVA IgG antibody to detect ovalbumin (OVA) as the antigen in ELISA. The enzymatic activity of (HRP)
4
–Stav was twofold higher than that of Stav–(HRP)
4
, and the sensitivity of (HRP)
4
-Stav in ELISA was higher than that of a commercial HRP–Stav chemical conjugate. The successful use of (HRP)
4
–Stav chimeric protein as a molecular probe in ELISA shows that the baculovirus-silkworm expression system is promising to produce enzyme–Stav conjugates to substitute for those prepared by chemical methods..
5. Jian Xu, Akihiro Morio, Daisuke Morokuma, Yudai Nagata, Masato Hino, Akitsu Masuda, Zhiqing Li, Hiroaki Mon, Takahiro Kusakabe, Man Lee, A functional polypeptide N-acetylgalactosaminyltransferase (PGANT) initiates O-glycosylation in cultured silkworm BmN4 cells, Applied Microbiology and Biotechnology, 10.1007/s00253-018-9309-6, 102, 20, 8783-8797, 2018.10, [URL], Mucin-type O-glycosylation is initiated by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts or PGANTs), attaching GalNAc to serine or threonine residue of a protein substrate. In the insect model from Lepidoptera, silkworm (Bombyx mori), however, O-glycosylation pathway is totally unexplored and remains largely unknown. In this study, as the first report regarding protein O-glycosylation analysis in silkworms, we verified the O-glycan profile that a common core 1 Gal (β1-3) GalNAc disaccharide branch without terminally sialylated structure is mainly formed for a baculovirus-produced human proteoglycan 4 (PRG4) protein. Intriguingly, functional screenings in cultured silkworm BmN4 cells for nine Bmpgants reveal that Bmpgant2 is the solo functional BmPGANT for PRG4, implying that Bmpgants may have unique cell/tissue or protein substrate preferences. Furthermore, a recombinant BmPGANT2 protein was successfully purified from silkworm-BEVS and exhibited a high ability to transfer GalNAc for both peptide and protein substrates. Taken together, the present results clarified the functional BmPGANT2 in cultured silkworm cells, providing crucial fundamental insights for future studies dissecting the detailed silkworm O-glycosylation pathways and productions of glycoproteins with O-glycans..
6. Patmawati xxxx, Kosuke Minamihata, Tsuneyuki Tatsuke, Man Lee, Takahiro Kusakabe, Noriho Kamiya, Expression and Activation of Horseradish Peroxidase–Protein A/G Fusion Protein in Silkworm Larvae for Diagnostic Purposes, Biotechnology Journal, 10.1002/biot.201700624, 13, 6, 2018.06, [URL], Recombinant protein production can create artificial proteins with desired functions by introducing genetic modifications to the target proteins. Horseradish peroxidase (HRP) has been used extensively as a reporter enzyme in biotechnological applications; however, recombinant production of HRP has not been very successful, hampering the utilization of HRP with genetic modifications. A fusion protein comprising an antibody binding protein and HRP will be an ideal bio-probe for high-quality HRP-based diagnostic systems. A HRP-protein A/G fusion protein (HRP-pAG) is designed and its production in silkworm (Bombyx mori) is evaluated for the first time. HRP-pAG is expressed in a soluble apo form, and is activated successfully by incubating with hemin. The activated HRP-pAG is used directly for ELISA experiments and retains its activity over 20 days at 4 °C. Moreover, HRP-pAG is modified with biotin by the microbial transglutaminase (MTG) reaction. The biotinylated HRP-pAG is conjugated with streptavidin to form a HRP-pAG multimer and the multimeric HRP-pAG produced higher signals in the ELISA system than monomeric HRP-pAG. The successful production of recombinant HRP in silkworm will contribute to creating novel HRP-based bioconjugates as well as further functionalization of HRP by applying enzymatic post-translational modifications..
7. Akitsu Masuda, Jian Xu, Kosuke Minamihata, Genki Kagawa, Yusei Hamada, Yoshiki Morifuji, Takumi Yano, Masato Hino, Daisuke Morokuma, Noriko Karasaki, Hiroaki Mon, Noriho Kamiya, Takahiro Kusakabe, Man Lee, Production of a biologically active human basic fibroblast growth factor using silkworm-baculovirus expression vector system, Journal of Asia-Pacific Entomology, 10.1016/j.aspen.2018.05.002, 21, 2, 716-720, 2018.06, [URL], As a therapeutic treatment, recombinant human basic fibroblast growth factor (rhbFGF) is usually employed in tissue regeneration, and as an essential component in culture medium for maintaining the induced pluripotent stem (iPS) cell and embryonic stem (ES) cell in an undifferentiated state. Therefore, a large amount of biologically active rhbFGF is required. In this study, silkworm-baculovirus expression vector system (silkworm-BEVS) is employed to achieve a high productivity of recombinant rhbFGF with two small affinity tags (His-tag and STREP-tag) at the N or C-terminus. It is observed that rhbFGF with 30 K signal peptide of silkworm were successfully expressed but are not sufficiently secreted into the culture medium of cultured insect cells. Then we purified the N- or C-tagged intracellular rhbFGF protein and obtained a yield of about 0.7 mg/larva and 1.2 mg/larva, respectively. Although the final yield of the C-tagged rhbFGF is higher than that of the N-tagged, rhbFGF with N-tag demonstrated promising and comparable biological activity, which is evaluated through a mammalian cell proliferation assay. Taken together, these results indicate that silkworm-BEVS could contribute to the mass-production of the biologically active rhbFGF for medical uses..
8. Mitsunori Shiroishi, Yuji Ito, Kenta Shimokawa, Man Lee, Takahiro Kusakabe, Tadashi Ueda, Structure–function analyses of a stereotypic rheumatoid factor unravel the structural basis for germline-encoded antibody autoreactivity, Journal of Biological Chemistry, 10.1074/jbc.M117.814475, 293, 18, 7008-7016, 2018.01, [URL], Rheumatoid factors (RFs) are autoantibodies against the fragment-crystallizable (Fc) region of IgG. In individuals with hematological diseases such as cryoglobulinemia and certain B cell lymphoma forms, the RFs derived from specific heavy- and light-chain germline pairs, so-called “stereotypic RFs,” are frequently produced in copious amounts and form immune complexes with IgG in serum. Of note, many structural details of the antigen recognition mechanisms in RFs are unclear. Here we report the crystal structure of the RF YES8c derived from the IGHV1-69/IGKV3-20 germline pair, the most common of the stereotypic RFs, in complex with human IgG1-Fc at 2.8 Å resolution. We observed that YES8c binds to the CH2–CH3 elbow in the canonical antigen-binding manner involving a large antigen–antibody interface. On the basis of this observation, combined with mutational analyses, we propose a recognition mechanism common to IGHV1-69/IGKV3-20 RFs: (1) the interaction of the Leu
432
–His
435
region of Fc enables the highly variable complementarity-determining region (CDR)-H3 to participate in the binding, (2) the hydrophobic tip in the CDR-H2 typical of IGHV1-69 antibodies recognizes the hydrophobic patch on Fc, and (3) the interaction of the highly conserved RF light chain with Fc is important for RF activity. These features may determine the putative epitope common to the IGHV1-69/IGKV3-20 RFs. We also showed that some mutations in the binding site of RF increase the affinity to Fc, which may aggravate hematological diseases. Our findings unravel the structural basis for germline-encoded antibody autoreactivity..
9. Akitsu Masuda, Man Lee, Takeshi Miyata, Tetsuo Sato, Shizuka Hayashi, Masato Hino, Daisuke Morokuma, Noriko Karasaki, Hiroaki Mon, Takahiro Kusakabe, Purification and characterization of immunogenic recombinant virus-like particles of porcine circovirus type 2 expressed in silkworm pupae, Journal of General Virology, 10.1099/jgv.0.001087, 99, 7, 917-926, 2018.01, [URL], Porcine circovirus type 2 (PCV2) is a primary causative agent of postweaningmultisystemic wasting syndrome (PMWS), which has a significant economic impact on the swine industry. The capsid protein (Cap) encoded by ORF2 of the viral genome has been used effectively as a vaccine against PCV2 infection. The Cap protein can spontaneously assemble into virus-like particles (VLPs) that are safe and highly immunogenic for vaccine applications. Several expression systems, including bacteria, yeast and insect cells, have been utilized to produce PCV2 VLPs. However, in some cases, the recombinant Cap (rCap) proteins produced in bacteria and yeast do not assemble spontaneously. In this study, we expressed rCap protein using a silkworm–baculovirus expression vector system (silkworm–BEVS) for mass production of PCV2 VLPs and established a simple three-step protocol for its purification from pupae: extraction by detergent, ammonium sulfate precipitation and anion exchange column chromatography. Size-exclusion chromatography (SEC) analysis and transmission electron microscope (TEM) observation showed that purified rCap proteins formed VLPs with a similar morphology to that of the original virus. Furthermore, the VLPs produced in silkworms were capable of inducing neutralizing antibodies against PCV2 in mice. Our results demonstrated that the silkworm system is a powerful tool for the production of PCV2 VLPs and will be useful for the development of a reliable and cost-effective PCV2 vaccine..
10. Akitsu Masuda, Kosuke Minamihata, Masato Hino, Daisuke Morokuma, Noriko Karasaki, Hiroaki Mon, Noriho Kamiya, Takahiro Kusakabe, Man Lee, Modular surface display for porcine circovirus type 2 virus-like particles mediated by microbial transglutaminase, Journal of Insect Biotechnology and Sericology, 10.11416/jibs.87.2_053, 87, 2, 53-60, 2018.01, [URL], Virus-like particles (VLPs) are multi-protein complex, which mimic viral particles without viral genomes. Recently various applications of VLPs for medical and pharmaceutical fields are developed. Furthermore, surface modification of VLPs is expected to extend their functional versatility. As an enzymatic strategy for the modification, microbial transglutaminase (MTG) that catalyzes the covalent bond between a glutamine residue and a ly-sine residue or a primary amine is suitable for efficient protein ligation. In the previous study, we demonstrated the efficient production of immunogenic VLPs of porcine circovirus type 2 (PCV2) using silkworm-baculovirus expression vector system (silkworm-BEVS). Herein, we established the display system of exotic molecules to VLPs by enzymatic covalent cross-linking using MTG. For the target modification, Q-tag (YPLQMRG) that is MTG reactive sequence were introduced into the N-terminus, C-terminus, or loop BC of capsid protein of PCV2 and successfully expressed as VLPs in silkworm pupae. Of these, PCV2 VLPs with Q-tag at the loop BC and C-terminus were efficiently conjugated with FITC-cadaverine and K-tagged (MRHKGS) EGFP by MTG. These results showed that flexible surface modification of VLPs mediated by MTG could be used for development of several therapeutic tools such as multivalent vaccines..
11. Yoshiki Morifuji, Jian Xu, Noriko Karasaki, Kazuhiro Iiyama, Daisuke Morokuma, Masato Hino, Akitsu Masuda, Takumi Yano, Hiroaki Mon, Takahiro Kusakabe, Man Lee, Expression, Purification, and Characterization of Recombinant Human α
1
-Antitrypsin Produced Using Silkworm–Baculovirus Expression System, Molecular Biotechnology, 10.1007/s12033-018-0127-y, 2018.01, [URL], Human α
1
-antitrypsin (AAT) is the most abundant serine proteinase inhibitor (serpin) in the human plasma. Commercially available AAT for the medications of deficiency of α
1
-antitrypsin is mainly purified from human plasma. There is a high demand for a stable and low-cost supply of recombinant AAT (rAAT). In this study, the baculovirus expression vector system using silkworm larvae as host was employed and a large amount of highly active AAT was recovered from the silkworm serum (~ 15 mg/10 ml) with high purity. Both the enzymatic activity and stability of purified rAAT were comparable with those of commercial product. Our results provide an alternative method for mass production of the active rAAT in pharmaceutical use..
12. Mami Yamashita, Jian Xu, Daisuke Morokuma, Kazuma Hirata, Masato Hino, Hiroaki Mon, Masateru Takahashi, Samir M. Hamdan, Kosuke Sakashita, Kazuhiro Iiyama, Yutaka Banno, Takahiro Kusakabe, Jae Man Lee, Characterization of Recombinant Thermococcus kodakaraensis (KOD) DNA Polymerases Produced Using Silkworm-Baculovirus Expression Vector System, Molecular Biotechnology, 10.1007/s12033-017-0008-9, 59, 6, 221-233, 2017.06, [URL], The KOD DNA polymerase from Thermococcus kodakarensis (Tkod-Pol) has been preferred for PCR due to its rapid elongation rate, extreme thermostability and outstanding fidelity. Here in this study, we utilized silkworm-baculovirus expression vector system (silkworm-BEVS) to express the recombinant Tkod-Pol (rKOD) with N-terminal (rKOD-N) or C-terminal (rKOD-C) tandem fusion tags. By using BEVS, we produced functional rKODs with satisfactory yields, about 1.1 mg/larva for rKOD-N and 0.25 mg/larva for rKOD-C, respectively. Interestingly, we found that rKOD-C shows higher thermostability at 95 °C than that of rKOD-N, while that rKOD-N is significantly unstable after exposing to long period of heat-shock. We also assessed the polymerase activity as well as the fidelity of purified rKODs under various conditions. Compared with commercially available rKOD, which is expressed in E. coli expression system, rKOD-C exhibited almost the same PCR performance as the commercial rKOD did, while rKOD-N did lower performance. Taken together, our results suggested that silkworm-BEVS can be used to express and purify efficient rKOD in a commercial way..
13. Daisuke Morokuma, Jian Xu, Masato Hino, Hiroaki Mon, Jasmeen S. Merzaban, Masateru Takahashi, Takahiro Kusakabe, Jae Man Lee, Expression and Characterization of Human β-1, 4-Galactosyltransferase 1 (β4GalT1) Using Silkworm–Baculovirus Expression System, Molecular Biotechnology, 10.1007/s12033-017-0003-1, 59, 4-5, 151-158, 2017.05, [URL], Baculovirus expression vector system (BEVS) is widely known as a mass-production tool to produce functional recombinant glycoproteins except that it may not be always suitable for medical practice due to the differences in the structure of N-linked glycans between insects and mammalian. Currently, various approaches have been reported to alter N-linked glycan structures of glycoproteins derived from insects into terminally sialylated complex-type N-glycans. In the light of those studies, we also proposed in vitro maturation of N-glycan with mass-produced and purified glycosyltransferases by silkworm–BEVS. β-1,4-Galactosyltransferase 1 (β4GalT1) is known as one of type II transmembrane enzymes that transfer galactose in a β-1, 4 linkage to accepter sugars, and a key enzyme for further sialylation of N-glycans. In this study, we developed a large-scale production of recombinant human β4GalT1 (rhβ4GalT1) with N- or C-terminal tags in silkworm–BEVS. We demonstrated that rhβ4GalT1 is N-glycosylated and without mucin-type glycosylation. Interestingly, we found that purified rhβ4GalT1 from silkworm serum presented higher galactosyltransferase activity than that expressed from cultured mammalian cells. We also validated the UDP-galactose transferase activity of produced rhβ4GalT1 proteins by using protein subtracts from silkworm silk gland. Taken together, rhβ4GalT1 from silkworms can become a valuable tool for producing high-quality recombinant glycoproteins with mammalian-like N-glycans..
14. Ming-Ming Ji, JAE MAN LEE, 門 宏明, Jian Xu, Tsuneyuki Tatsuke, takahiro kusakabe, Proteasome inhibitor MG132 impairs autophagic flux through compromising formation of autophagosomes in Bombyx cells, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 10.1016/j.bbrc.2016.09.151, 479, 4, 690-696, 2016.10.
15. Jianping Chen, Jian Xu, Masato Hino, Mami Yamashita, Kazuma Hirata, Anandrao Ashok Patil, Tsuneyuki Tatsuke, 門 宏明, Banno Y, takahiro kusakabe, JAE MAN LEE, Co-expression of silkworm allatostatin-C receptor BNGR-A1 with its cognate G protein subunits enhances the GPCR display on the budding baculovirus, Journal of Asia-Pacific Entomology, 10.1016/j.aspen.2016.07.007, 19, 3, 753-760, 2016.09.
16. Ji-Hyun Choi, Dae-Jung Kim, Sun Mee Hong, Sun-Jung Jo, Kwan-Sik Min, Young Chang Sohn, JAE MAN LEE, takahiro kusakabe, Molecular analysis and bioactivity of luteinizing hormone from Japanese eel, Anguilla japonica, produced in silkworm pupae, BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, 10.1007/s12257-016-0042-7, 21, 3, 381-388, 2016.06.
17. Kazuhiro Iiyama, JAE MAN LEE, Tsuneyuki Tatsuke, 門 宏明, takahiro kusakabe, Expression and Characterization of Recombinant Serratia liquefaciens Nucleases Produced with Baculovirus-mediated Silkworm Expression System, MOLECULAR BIOTECHNOLOGY, 10.1007/s12033-016-9937-y, 58, 6, 393-403, 2016.06.
18. Masato Hino, Daisuke Morokuma, 門 宏明, JAE MAN LEE, takahiro kusakabe, Characterization of the roles of DNA polymerases, clamp, and clamp loaders during S-phase progression and cell cycle regulation in the silkworm, Bombyx mori, Journal of Insect Biotechnology and Sericology, 85, 21-29, 2016.06.
19. Masato Hino, Takuji Kawanami, Jian Xu, Daisuke Morokuma, Kazuma Hirata, Mami Yamashita, Noriko Karasaki, Tsuneyuki Tatsuke, 門 宏明, Kazuhiro Iiyama, 神谷 典穂, Banno Y, takahiro kusakabe, JAE MAN LEE, High-level expression and purification of biologically active human IL-2 using silkworm-baculovirus expression vector system., Journal of Asia-Pacific Entomology, 10.1016/j.aspen.2016.03.014, 19, 313-317, 2016.06.
20. Jian Xu, Pingbo Zhang, takahiro kusakabe, 門 宏明, Zhiqing Li, Li Zhu, Kazuhiro Iiyama, YUTAKA BANNO, Daisuke Morokuma, JAE MAN LEE, Comparative proteomic analysis of hemolymph proteins from Autographa californica multiple nucleopolyhedrovirus (AcMNPV)-sensitive or -resistant silkworm strains during infections, COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY D-GENOMICS & PROTEOMICS, 10.1016/j.cbd.2015.07.003, 16, 36-47, 2015.12.
21. Saki Imai, takahiro kusakabe, Jian Xu, Zhiqing Li, Shintaro Shirai, 門 宏明, Daisuke Morokuma, JAE MAN LEE, Roles of silkworm endoplasmic reticulum chaperones in the secretion of recombinant proteins expressed by baculovirus system, MOLECULAR AND CELLULAR BIOCHEMISTRY, 10.1007/s11010-015-2529-5, 409, 1-2, 255-262, 2015.11.
22. Kounosuke Hayashi, JAE MAN LEE, Yusuke Tomozoe, takahiro kusakabe, 神谷 典穂, Heme precursor injection is effective for Arthromyces ramosus peroxidase fusion protein production by a silkworm expression system, JOURNAL OF BIOSCIENCE AND BIOENGINEERING, 10.1016/j.jbiosc.2015.02.013, 120, 4, 384-386, 2015.10.
23. Atsushi Masuda, Jian Xu, Takumi Mitsudome, Yudai Nagata, Daisuke Morokuma, 門 宏明, YUTAKA BANNO, takahiro kusakabe, JAE MAN LEE, Mass Production of an Active Peptide-N-Glycosidase F Using Silkworm-Baculovirus Expression System, MOLECULAR BIOTECHNOLOGY, 10.1007/s12033-015-9866-1, 57, 8, 735-745, 2015.08.
24. Yasuyuki Hashiguchi, JAE MAN LEE, M. Shiraishi, S. Komatsu, S. Miki, Yohei Shimasaki, N. Mochioka, Yuji Oshima, takahiro kusakabe, Characterization and evolutionary analysis of tributyltin‐binding protein and pufferfish saxitoxin and tetrodotoxin‐binding protein genes in toxic and nontoxic pufferfishes, Journal of evolutionary biology, 28, 5, 1103-1108, 2015.05.
25. Daisuke Morokuma, 門 宏明, Banno Y, takahiro kusakabe, JAE MAN LEE, Differential N-Glycan Modifications of Human Alpha 1-Acid Glycoprotein (α1AGP) Produced in Different Silkworm Strains using the Baculovirus Expression System, Journal of Insect Biotechnology and Sericology, 84, 2, 49-53, 2015.05.
26. Daisuke Morokuma, Jian Xu, 門 宏明, Kazuma Hirata, Masato Hino, Shoko Kuboe, Mami Yamashita, takahiro kusakabe, JAE MAN LEE, Human alpha 1-acid glycoprotein as a model protein for glycoanalysis in baculovirus expression vector system, Journal of Asia-Pacific Entomology, 18, 2, 303-309, 2015.06.
27. Atsushi Masuda, Jian Xu, Takumi Mitsudome, Daisuke Morokuma, 門 宏明, YUTAKA BANNO, takahiro kusakabe, JAE MAN LEE, Improvement of Endo-β-N-acetylglucosaminidase H production using silkworm–baculovirus protein expression system, Journal of Asia-Pacific Entomology, 18, 2, 175-180, 2015.06.
28. Jian Xu, takahiro kusakabe, Kimiko Yamamoto, Yoshitaka Suetsugu, 門 宏明, Zhiqing Li, Li Zhu, Kazuhiro Iiyama, YUTAKA BANNO, Kaito Yoshimura, JAE MAN LEE, A novel third chromosomal locus controls susceptibility to Autographa californica multiple nucleopolyhedrovirus in the silkworm, Bombyx mori., Applied Microbiology and Biotechnology, 98, 7, 3049-3058, 2014.04.
29. JAE MAN LEE, Jian Xu, 門 宏明, Takumi Mitsudome, Atsushi Masuda, Kaito Yoshimura, Kazuhiro Iiyama, Yuuka Chieda, takahiro kusakabe, Baculovirus-mediated gene transfer systems in silkworm larvae using constitutive host promoters, JOURNAL OF ASIA-PACIFIC ENTOMOLOGY, 10.1016/j.aspen.2013.10.009, 17, 1, 73-78, 2014.03.
30. Yudai Nagata, JAE MAN LEE, 門 宏明, Shigeo Imanishi, Sun Mee Hong,, Shoji Komatsu, Yuji Oshima, takahiro kusakabe, RNAi suppression of β-N-acetylglucosaminidase (BmFDL) for complex-type N-linked glycan synthesis in cultured silkworm cells, Biotechnology letters, 10.1007/s10529-013-1183-9, 35, 7, 1009-1016, 2013.07.
31. Tsuneyuki Tatsuke, JAE MAN LEE, takahiro kusakabe, Kazuhiro Iiyama, Hideki Sezutsu, Keiro Uchino, TIGHTLY CONTROLLED TETRACYCLINE-INDUCIBLE TRANSCRIPTION SYSTEM FOR EXPLOSIVE GENE EXPRESSION IN CULTURED SILKWORM CELLS, ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY, 10.1002/arch.21083, 82, 4, 173-182, 2013.04.
32. Jian Xu, Yudai Nagata, 門 宏明, Zhiqing Li, Li Zhu, Kazuhiro Iiyama, takahiro kusakabe, JAE MAN LEE, Soaking RNAi-mediated modification of Sf9 cells for baculovirus expression system by ectopic expression of Caenorhabditis elegans SID-1, Applied Microbiology and Biotechnology, 2013.03.
33. JAE MAN LEE, Yoshito Kojin, Tsuneyuki Tatsuke, 門 宏明, Yoshitaka Miyagawa, takahiro kusakabe, Coexpression of Escherichia coli RNase III in silkworm cells improves the efficiency of RNA interference induced by long hairpin dsRNAs, Insect Science, 10.1111/j.1744-7917.2012.01569.x, 20, 1, 69-77, 2013.02.
34. Zhiqing Li, Daojun Cheng, 門 宏明, Li Zhu, Jian Xu, Tsuneyuki Tatsuke, JAE MAN LEE, Qingyou Xia, takahiro kusakabe, Cell Cycle-Dependent Recruitment of Polycomb Proteins to the ASNS Promoter Counteracts C/ebp-Mediated Transcriptional Activation in Bombyx mori, PloS one, 10.1371/journal.pone.0052320, 8, 1, e52320, 2013.01.
35. Mai Fukushima, Kazuhiro Iiyama, Jun Yamashita, Masutaka Furue, Gaku Tsuji, Shigeo Imanishi, 門 宏明, JAE MAN LEE, takahiro kusakabe, PRODUCTION OF SMALL ANTIBACTERIAL PEPTIDES USING SILKWORM-BACULOVIRUS PROTEIN EXPRESSION SYSTEM, Preparative Biochemistry and Biotechnology, 2013.01.
36. Yasuhiko Soejima, JAE MAN LEE, Yudai Nagata, 門 宏明, Kazuhiro Iiyama, 北野 載, Michiya Matsuyama, takahiro kusakabe, Comparison of signal peptides for efficient protein secretion in the baculovirus-silkworm system, Central European Journal of Biology, 10.2478/s11535-012-0112-6, 8, 1, 1-7, 2013.01.
37. 門 宏明, JAE MAN LEE, Mai Fukushima, Yudai Nagata, Mie Fuji, Jian Xu, Oumi Nishi, Kazuhiro Iiyama, takahiro kusakabe, Production and characterization of the celery mismatch endonuclease CEL II using baculovirus/silkworm expression system, Applied microbiology and biotechnology, 2012.11.
38. Hitoshi Kurio, JAE MAN LEE, takahiro kusakabe, hiroshi iida, Testis-specific Cell Adhesion Molecule, CEACAM6-L, Forms Homophilic Interaction at the Cell Adhesion Site in Vitro, Zoological science, 10.2108/zsj.29.786, 29, 11, 786-793, 2012.11.
39. JAE MAN LEE, Naoya Kawakami, 門 宏明, Hitoshi Mitsunobu, Kazuhiro Iiyama, Satoshi Ninaki, Katsumi Maenaka, Enoch Y Park, takahiro kusakabe, Establishment of a Bombyx mori nucleopolyhedrovirus (BmNPV) hyper-sensitive cell line from the silkworm e21 strain, Biotechnology letters, 10.1007/s10529-012-0971-y, 34, 10, 1773-1779, 2012.10.
40. JAE MAN LEE, Yoshito Kojin, Tsuneyuki Tatsuke, 門 宏明, Yoshitaka Miyagawa, takahiro kusakabe, RNA Interference Induction by Long Hairpin dsRNAs Expressed from Chromosomal DNA of Bombyx mori Cells, Journal of the Faculty of Agriculture, Kyushu University, 57, 2, 441-445, 2012.09.
41. Lee, J.M., Mon, H., Banno, Y., Iiyama, K., Kusakabe, T., Bombyx mori strains useful for efficient recombinant protein production using a baculovirus vector., J. Biotech. Biomater., 2012.06.
42. Zhu, L., Tatsuke, T., Li, Z., Mon, H., Xu, Z., Lee, J.M., and Kusakabe T.,, Molecular cloning of BmTUDOR-SN and analysis of its role in RNAi pathway in the silkworm, Bombyx mori (Lepidoptera: Bombycidae). , Appl. Entomol. Zool., 2012.06.
43. Sugahara, R., Mon, H., Lee, J.M., and Kusakabe, T.,, Monoubiquitination-Dependent Chromatin Loading of FancD2 in Silkworms, a Species Lacking the FA Core Complex., Gene, 2012.05.
44. Fujii, M., Takahashi, M., Mon, H., Tatsuke, T., Lee, J.M, and Kuskabe T. , Molecular cloning of the silkworm p53R2 homolog gene. , J. Fac. Agr. Kyushu Univ., , 57, 79-82, 2012.04.
45. Nagata, Y., Sakashita, K., Imanishi, S., Lee, J.M., and Kuskabe T. , Expression of glycosylated mucin-like domain using baculovirus expression system in silkworm, Bombyx mori., J. Fac. Agr. Kyushu Univ., , 57, 83-86, 2012.04.
46. Li, Z., Cheng, D., Mon, H., Tatsuke, T., Zhu, L., Xu, J., Lee, J.M., Xia, Q., and Kusakabe, T., Genome-wide identification of Polycomb target genes reveals a functional association of Pho with Scm in Bombyx mori., PLoS ONE, , 7, e34330, 2012.01.
47. Mon, H., Kobayashi, I., Ohkubo, S. Tomita, S., Lee, J.M., Sezutsu, H., Tamura, T., Kusakabe, T., Effective RNA interference in cultured silkworm cells mediated by overexpression of Caenorhabditis elegans SID-1., RNA Biol., , 9, 40-46, 2012.01.
48. Mitsunobu, H., Izumi, H., Mon, H., Tatsuke, T., Lee, J.M., Kusakabe, T., Molecular Characterization of heterochromatin proteins 1a and 1b from the Silkworm, Bombyx mori., Insect Mol. Biol. , 21, 9-20, 2012.01.
49. Mon, H., Izumi, M., Mitsunobu, H., Tatsuke, T., Iiyama, K., Jikuya, H., Lee, J.M., Kusakabe, T., Post-translational modifications of the N-terminal tail of histone H3 in holocentric chromosomes of bombyx mori. Insect Biochem. , Mol. Genet. Genomics, 2011.09.
50. Mon, H., Lee, J.M., Kawaguchi, Y., Kusakabe, T., Double-strand breaks repair by gene conversion in silkworm holocentric chromosomes, Mol. Genet. Genomics, 2011.09.
51. Kawakami, N., Lee, J.M., Mon, H., Kubo, Y., Banno, Y., Kawaguchi, Y., Maenaka, K., Park, E.Y., Koga, K. and Kusakabe, T., Efficient protein expression in Bombyx mori larvae of the strain d17 highly sensitive to B. mori nucleopolyhedrovirus., Mol Biotechnol. , 40(2), 180-185 , 2008.02.
52. Lee JM, Takahashi M, Mon H, Mitsunobu H, Koga K, Kawaguchi Y, Nakajima Y, Kusakabe T., Construction of gene expression systems in insect cell lines using promoters from the silkworm, Bombyx mori., J Biotechnol, 133(1) 9-17 , 2008.02.
53. Lee J.M., Mon H., Takahashi M., Kawakami N. Yoshida Y., Banno Y., Koga K., Kawaguchi Y. and Kusakabe T. , Screening of high-permissive silkworm strains for efficient recombinant protein production in Autographa californica nuclear polyhedrosis virus (AcNPV). , J. Insect Biotech. Seric. , In press, 2007.03.
54. Lee J.M., Takahashi M., Mon H., Koga K., Kawaguchi Y., and Kusakabe T., Efficient gene transfer into silkworm larval tissues by a combination of sonoporation and lipofection., Cell Biol. Int., 10.1016/j.cellbi.2005.07.007, 29, 11, 976-979, 29, 976-979., 2005.01.
主要学会発表等
1. 増田亮津,宮田健,南畑孝介,神谷典穂,李在萬,日下部宜宏, 昆虫工場を用いたウイルス様粒子ワクチンの生産系の確立とその応用, 第71回日本衛生動物学会大会, 2019.04.
2. 増田亮津,南畑孝介,神谷典穂,李在萬,日下部宜宏, カイコ生産ウイルス様粒子表面への抗原ディスプレイの試み, 平成31年蚕糸学会本会, 2019.03.
3. 増田亮津,唐崎紀子,伴野 豊,南畑孝介,神谷典穂,門宏明,李在萬,日下部宜宏, カイコ-バキュロウイルス発現系を用いた組換えヒト血管内皮細胞増殖因子の高効率生産, 第41回日本分子生物学会, 2018.11.
4. 李在萬, 昆虫工場におけるVLP生産, 昆虫ポストゲノム研究会, 2018.10.
5. 増田亮津、木下友里恵、森尾明大、宮田健、神谷典穂、李在萬、日下部宜宏, 部位特異的架橋技術を用いたカイコ生産ウイルス様粒子表面への分子ディスプレイ, 平成30年蚕糸学会本会, 2018.03.
6. Akitsu Masuda, Yurie Kinoshita, Akihiro Morio, Takeshi Miyata, Jae Man Lee, Takahiro Kusakabe, Characterization of Porcine Circovirus Type 2 Virus-like Particles produced by Silkworm-baculovirus Expression Vector System, International Symposium on Agricultural, Food, Environmental and Life Sciences in Asia 2017, 2017.11.
7. Akitsu Masuda, Yurie Kinoshita, Akihiro Morio, Noriko Karasaki, Tsuneyuki Tatsuke, Hiroaki Mon, Kosuke Minamihata, Noriho Kamiya, Jae Man Lee, Takahiro Kusakabe, High-yield Production of Biologically Active Human Basic Fibroblast Growth Factor Using Silkworm-baculovirus Expression Vector System, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2017.03.
8. Ming-Ming Ji, JAE MAN LEE, 門 宏明, Zhiqing Li, Jian Xu, Li Zhu, Takahiro Kusakabe, Lipidation, delipidation and degradation of Atg8 in Bombyx cells, 平成27年蚕糸学会本会, 2016.03.
9. 諸熊大輔, 徐剣, 門 宏明, 李在萬, 日下部 宜宏, ヒト糖転移酵素の導入によるカイコ培養細胞のN型糖鎖修飾改変の試み, 平成27年蚕糸学会本会, 2016.03.
10. 門 宏明, JAE MAN LEE, Takahiro Kusakabe, Novel kinetochore protein complex from silkworm holocentric chromosomes, 29th Annual Symposiumof the Protein Society , 2015.07.
11. 門 宏明, 李在萬, 日下部宜宏, カイコ分散型動原体を構成するタンパク質の解析, 日本分子生物学会本会, 2015.12.
12. 諸熊大輔, 門 宏明, 李在萬, 伴野豊, 日下部宜宏, カイコバキュロウイルス発現系を用いたヒト糖転移酵素の大量生産, 日本分子生物学会本会, 2015.12.
13. Jian Xu, 門 宏明, JAE MAN LEE, Takahiro Kusakabe, RNA-Seq-based transcriptome analysis of p38, ERK and JNK MAPK gene suppressions in cultured Bombyx mori cells, 日本分子生物学会本会, 2015.12.
14. Masato Hino, JAE MAN LEE, Mami Yamashita, Kazuma Hirata, Daisuke Morokuma, Takahiro Kusakabe, Expression and Purification of IL-1b related proteins Using Silkworm Baculovirus Protein Expression System, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2015.04.
15. Masato Hino, Takumi Mitsudome, 門 宏明, Masanao Sato, Yoshitaka Suetsugu, Kimiko Yamamoto, Zhiqing Li, Jian Xu, Li Zhu, JAE MAN LEE, Takahiro Kusakabe, DNA methyltransferase DNMT-1 from Bombyx mori, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2015.04.
16. Kazuma Hirata, JAE MAN LEE, Jian Xu, Masato Hino, Mami Yamashita, 門 宏明, Takahiro Kusakabe, Expression and Purification of Fibroblast Growth Factors 1, 7, and 10 from Silkworm-Baculovirus Expression Vector System, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2015.04.
17. Daisuke Morokuma, 門 宏明, JAE MAN LEE, Takahiro Kusakabe, YUTAKA BANNO, Expression, purification, and characterization of human alpha 1 acid glycoprotein (α1AGP) for glycobiological research in baculovirus expression system, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2015.04.
18. Daisuke Morokuma, 門 宏明, JAE MAN LEE, Takahiro Kusakabe, YUTAKA BANNO, Expression and characterization of short-type human alpha 1 acid glycoprotein (α1AGP∆) for glycobiological research in baculovirus expression system, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2015.04.
19. Kazuma Hirata, Atsushi Masuda, JAE MAN LEE, 門 宏明, Takahiro Kusakabe, Efficient Endo H expression by silkworm baculovirys expression system, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2015.04.
20. Mami Yamashita, Masato Hino, Kazuma Hirata, Jian Xu, Mingming Ji, Daisuke Morokuma, 門 宏明, JAE MAN LEE, Takahiro Kusakabe, Expression, purification, and characterization of streptavidin mutants using Baculovirus-mediated silkworm protein expression system, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2015.04.
21. Mami Yamashita, Jian Xu, JAE MAN LEE, 門 宏明, Takahiro Kusakabe, Improvement of Caenorhabditis elegans SID-1-Dependent DNA Delivery System in Cultured Silkworm Cells, International Symposium on Basic and Applied Research on Sericulture and Insect Sciences, 2015.04.
22. Masato Hino, 門 宏明, Li Zhu, Mami Yamashita, Kazuma Hirata, Dan Zheng, Jian Xu, Ming-Ming Ji, Daisuke Morokuma, JAE MAN LEE, Takahiro Kusakabe, Characterization of silkworm replication related proteins for making an artificial chromosome, The 4th Asia-Pacific Congress of Sericulture and Insect Biotechnology, 2015.04.
23. Mami Yamashita, Masato Hino, Kazuma Hirata, Jian Xu, Ming-Ming Ji, Daisuke Morokuma, 門 宏明, JAE MAN LEE, Takahiro Kusakabe, Characterization of BmNPV Promoters for Improving Exogenous Genes Expression in Bombyx Cells, The 4th Asia-Pacific Congress of Sericulture and Insect Biotechnology, 2015.04.
24. Kazuma Hirata, JAE MAN LEE, Jian Xu, Masato Hino, Mami Yamashita, 門 宏明, Takahiro Kusakabe, Establishiment of New insect Cell Lines by Using Cell Fusion Method, The 4th Asia-Pacific Congress of Sericulture and Insect Biotechnology, 2015.04.
25. Daisuke Morokuma, Jian Xu, 門 宏明, JAE MAN LEE, Takahiro Kusakabe, Synthesis of Complex-Type N-Glycans on Recombinant Proteins by Modifying N-Glycosylation Pathway in Cultured Silkworm Cells, The 4th Asia-Pacific Congress of Sericulture and Insect Biotechnology, 2015.04.
26. Ming-Ming Ji, JAE MAN LEE, 門 宏明, Zhiqing Li, Jian Xu, Li Zhu, Shoko Kuboe, Saki Imai, Jianping Chen, Takumi Mitsudome, Atsushi Masuda, Daisuke Morokuma, Masato Hino, Mami Yamashita, Kazuma Hirata, Takahiro Kusakabe, GFP-p62 degradation is an excellent marker of autophagic flux in Bombyx, The 4th Asia-Pacific Congress of Sericulture and Insect Biotechnology, 2015.04.
27. Jianping Chen, Jian Xu,, Li Zhu, JAE MAN LEE, Takahiro Kusakabe, Engineering of silkworm-baculovirus expression system for efficient production of G protein -coupled receptors, The 4th Asia-Pacific Congress of Sericulture and Insect Biotechnology, 2015.04.
28. 平田一真, 佐藤昌直, 徐剣, 季明明, 祝力, 日野真人, 山下真実, 諸熊大輔, 門 宏明, 李在萬, 日下部 宜宏, カイコにおけるTORシグナル経路の解明, 平成27年蚕糸学会本会, 2015.09.
29. 日野真人, 門 宏明, 徐剣, 祝力, 李在萬, 日下部 宜宏, カイコ複製関連遺伝子の網羅的ノックダウ ン解析, 平成27年蚕糸学会本会, 2015.09.
30. 山下真実, 徐剣, 季明明, 門 宏明, 李在萬, 日下部 宜宏, カイコ培養細胞におけるBmNPV 136遺伝子のプロモーター活性, 平成27年蚕糸学会本会, 2015.09.
31. 諸熊 大輔, 日下部 宜宏, 李 在萬, 門 宏明, 伴野 豊, ヒトα1-酸性糖タンパク質(α1AGP)は昆虫細胞における糖鎖生物学研究のモデルタンパク質となる, 平成26年第37回日本分子生物学会本会, 2014.11.
32. Saki Imai, Jian Xu,, Hiroaki Mon, JAE MAN LEE, Takahiro Kusakabe, Function of silkworm XBP1 during an ER stress response, 平成26年第37回日本分子生物学会本会, 2014.11.
33. Takumi Mitsudome, Hiroaki Mon, Masanao Sato, Yoshitaka Suetsugu, Kimiko Yamamoto, Zhiqing Li, Jian Xu,, Li Zu, JAE MAN LEE, Takahiro Kusakabe, Atsushi Masuda, Biochemical characterization of Bombyx mori DNA methyltransferase-1 (BmDNMT-1) and its roles on transcriptional regulation, 平成26年第37回日本分子生物学会本会, 2014.11.
34. 祝力, 徐剣, 李志清, 門 宏明, LEE JAE MAN, 日下部 宜宏, Role of silkworm RISC components in the basal defense against Bombyx mori nucleopolyhedrovirus (BmNPV), 平成26年蚕糸学会本会, 2014.03.
35. 門 宏明, LEE JAE MAN, 日下部 宜宏, カイコ動原体を構成するタンパク質の解析, 平成26年蚕糸学会本会, 2014.03.
36. 日下部 宜宏, 門 宏明, LEE JAE MAN, Xu Jian, Li Zhiqing, Soaking RNAi and its application on insect sciences, 25年韓国蚕糸学会本会(大韓民国平昌郡), 2013.05.
37. 益田篤, 佐藤昌直, 末次克行, 山本公子, 門 宏明, LEE JAE MAN, 日下部 宜宏, カ イコ分散型動原体ループドメイン形成への CTCF, CP190 の関与, 平成25年蚕糸学会本会, 2013.03.
38. 満留卓実, 門 宏明, 佐藤昌直, 末次克行, 山本公子, 李志清, 徐剣, 祝力, LEE JAE MAN, 日下部 宜宏, BmDnmt1, BmDnmt2, bMBDの機能阻害細胞におけるDNAのメチル化, 平成25年蚕糸学会本会, 2013.03.
39. 福島舞, 飯山 和弘, LEE JAE MAN, 山下隼, 門 宏明, 古江増隆, 辻学, 日下部 宜宏, カイコ BES を用いたヒト β-defensin (DEFB)-1, 2, 3 と LL37 の発現と抗菌活性の測定, 平成24年第35回日本分子生物学会本会, 2012.12.
40. 永田祐大, 門 宏明, LEE JAE MAN, 日下部 宜宏, カイコ培養細胞による多分岐型N-グリカンを持つ糖タンパク質の生産, 平成24年第35回日本分子生物学会本会, 2012.12.
41. 藤井美江, 門 宏明, 高橋将晃, 光延仁志, LEE JAE MAN, 日下部 宜宏, カイコ培養細胞NHEJにおける修復関連遺伝子ノックダウンの影響, 平成24年第35回日本分子生物学会本会, 2012.12.
42. 吉村開人, 田附 常幸, 門 宏明, LEE JAE MAN, 日下部 宜宏, カイコにおけるヒストンH3S10リン酸化の役割, 平成24年第35回日本分子生物学会本会, 2012.12.
43. 満留卓実, 門 宏明, 徐剣, LEE JAE MAN, 日下部 宜宏, カイコにおけるDNAメチル化因子の機能解析, 平成24年第35回日本分子生物学会本会, 2012.12.
44. 益田篤, 佐藤昌直, 門 宏明, LEE JAE MAN, 日下部 宜宏, カイコ分散型動原体染色体におけるクロマチンループ形成とその役割, 平成24年第35回日本分子生物学会本会, 2012.12.
45. Zhiqing Li・Hiroaki Mon・Jae Man Lee・Takahiro Kusakabe, Molecular cloning and characterization of asparagine synthetase in the silkworm, Bombyx mori, 平成24年蚕糸学会本会, 2012.03.
46. 吉末真吾・田附常幸・阪下浩介・門 宏明・李 在萬・日下部宜宏, カイコにおける RNAi 経路の解析, 平成24年蚕糸学会本会, 2012.03.
47. Li Zhu・Tuneyuki Tatsuke・Hiroaki Mon・Jae Man Lee・Takahiro Kusakabe, BmTudor-sn interact with BmAgo1 and BmAgo2 not to be involved in RNAi pathway, while to participate in stress granule formation in BmN4 cells, 平成24年蚕糸学会本会, 2012.03.
48. 吉村開人・田附常幸・門 宏明・李 志清・李 在萬・日下部宜宏, 点変異導入によるカイコヒストン H3-K4, K9, K27, S10 修飾の機能解析, 平成24年蚕糸学会本会, 2012.03.
49. 藤井美江・門 宏明・高橋将晃・光延 仁・李 在萬・日下部宜宏, カイコにおける DNA 二重鎖切断関連因子の解析, 平成24年蚕糸学会本会, 2012.03.
50. Jian Xu・Kimito Yamamoto・Hiroaki Mon・Jae Man Lee・Takahiro Kusakabe, Positional cloning and functional analysis of candidate genes responsible for AcNPV sensitivity in silkworm, Bombyx mori, 平成24年蚕糸学会本会, 2012.03.
51. 副嶋泰彦・李 在萬・日下部宜宏, カイコ培養細胞における糖鎖修飾部位改変組換え分泌タンパク質の生産, 平成24年蚕糸学会本会, 2012.03.
52. 工藤遼亮・日下部宜宏・李 在萬・門 宏明, BES におけるタンパク質分泌量への小胞体シャペロンの関与, 平成24年蚕糸学会本会, 2012.03.
53. 福島 舞・飯山和弘・李 在萬・山下 隼・古江増隆・辻 学・日下部宜宏, カイコ BES によるヒト DEFB1, 2, 3 と LL37 の発現と DEFB2 が菌の生存率に与える影響, 平成24年蚕糸学会本会, 2012.03.
54. 永田祐大・副嶋泰彦・門 宏明・李 在萬・日下部宜宏, カイコ培養細胞における N-グリコシル化経路の改変とタンパク質発現系への応用, 平成24年蚕糸学会本会, 2012.03.
55. 門宏明・李在萬・日下部宜宏, カイコにおける分散型動原体タンパク質の解析/Analysis of the kinetochore proteins in holocentric chromosomes of Bombyx mori, 平成23年第34回日本分子生物学会本会, 2011.12.
56. 田附常幸・藤井美江・永田祐大・福島舞・李在萬・日下部宜宏, カイコにおけるテトラサイクリン誘導型遺伝子発現システムの改良/Improvement of tetracycline-inducible gene expression systems in the silkworm, Bombyx mori, 平成23年第34回日本分子生物学会本会, 2011.12.
57. 祝力・田附常幸・李志清・門宏明・李在萬・日下部宜宏, Analysis of P-bodies and stress granules in silkworm BmN4 cells, 平成23年第34回日本分子生物学会本会, 2011.12.
58. 工藤遼亮・門宏明・李在萬・日下部宜宏, バキュロウイルス発現系における小胞体シャペロンの関与/Roles of the endoplasmic reticulam chaperones in recombinant protein secretion in BES, 平成23年第34回日本分子生物学会本会, 2011.12.
59. 永田祐大・副嶋泰彦・門宏明・李在萬・日下部宜宏, カイコ β-N-acetylglucosaminidase (BmFDL) のノックダウンが N- グリカン形成に与える影響/Effect of RNAi for BmFDL in the N-glycosylation pathway, 平成23年第34回日本分子生物学会本会, 2011.12.
60. 福島舞・飯山和弘・李在萬・山下隼・古江増隆・辻学・日下部宜宏, カイコ BES を用いたヒト抗菌タンパク質の生産と活性評価/Production of human antimicrobial peptides using baculovirus expression system and evaluation of its activity, 平成23年第34回日本分子生物学会本会, 2011.12.
61. 藤井美江、門宏明、高橋将晃、光延仁志、李在萬、日下部宜宏, カイコ培養細胞におけるDNA二重鎖切断修復経路の解析/Analysis of DNA double-strand break repair pathways in silkworm cells, 平成23年第34回日本分子生物学会本会, 2011.12.
62. 門宏明・李在萬・日下部宜宏, カイコ動原体タンパク質の解析, 平成23年蚕糸学会本会, 2011.03.
63. 菅原亮平・門宏明・李在萬・日下部宜宏, カイコにおけるフアンコニ経路因子FancMの機能解析, 平成23年蚕糸学会本会, 2011.03.
64. 山下隼・福島舞・李在萬・日下部宜宏, カイコ熱ショックファクターBmHsf1, BmHsf1lpの転写活性化機構に関する研究, 平成23年蚕糸学会本会, 2011.03.
65. 永田祐大・副嶋泰彦・門宏明・李在萬・日下部宜宏, 糖鎖構造の改変によるカイコーバキュロウイルス発現系への応用, 平成23年蚕糸学会本会, 2011.03.
66. Takahiro Kusakabe, JaeMan Lee, Efficient Protein Expression in Bombyx mori Larvae of the Strains Highly Sensitive to B. mori Nucleopolyhedrovirus, The bioprocessing summit 2010: Baculovirus Technology, 2010.08.
67. 管原亮平・門宏明・李在萬・河口豊・日下部宜宏,, カイコにおけるDNA損傷修復機構ファンコニ経路の解析, 平成22年蚕糸学会本会, 2010.04.
68. 田附常幸・光延仁志・正木夕輝・阪下浩介・吉末真吾・李在萬・河口豊・日下部宜宏, カイコ培養細胞 BmN4 における Piwi サブファミリータンパク質の転写抑制への関与, 平成22年蚕糸学会本会, 2010.04.
69. Ryohei Sugahara, Hiroaki Mon, Jae Man Lee, and Takahiro Kusakabe, Molecular characterization of the Fanconi anemia protein FancM in silkworm, Bombyx mori, 平成22年日本分子生物学会本会, 2010.12.
70. 田附常幸、正木夕輝、吉末真吾、光延仁志、阪下浩介、李在萬、日下部宜宏, カイコ Piwi タンパク質による転写抑制効果の解析, 平成22年日本分子生物学会本会, 2010.12.
71. Zhiqing Li, Tsuneyuki Tatsuke, Hiroaki Mon, JaeMan Lee, and Takahiro Kusakabe, Identification and Expression Pattern Analysis of Polycomb Group Genes in the Silkworm, Bombyx mori,, 平成22年日本分子生物学会本会, 2010.12.
72. Yuki Masaki, Tsuneyuki Tatsuke, Kosuke Sakashita, Shingo Yoshizue, JaeMan Lee, and Takahiro Kusakabe, Silkworm Argonaute2 homolog is involved in exso-siRNA and endo-siRNA pathway, 平成22年日本分子生物学会本会, 2010.12.
73. Ryosuke Kudo,Jun Yamashita,Hiroaki Mon,Jae Man Lee and Takahiro Kusakabe, BESにおけるタンパク質分泌量への小胞体シャペロンの関与, 平成22年日本分子生物学会本会, 2010.12.
74. 吉末 真吾,田附 常幸,正木 夕輝,阪下 浩介,李 在萬,日下部 宜宏, カイコ Dicer-2 のクローニングと機能解析, 平成22年日本分子生物学会本会, 2010.12.
75. Jun Yamashita, Hiroaki Mon, Hitoshi Mitsunobu, Shun Sawatsubashi, Shigeaki Kato, Jae Man Lee, Yutaka Kawaguchi, Takahiro Kusakabe, Functional analysis of BmHsp90 cochaperones for hormone receptors in the silkworm., 平成21年日本分子生物学会本会, 2009.12.
76. Hiroaki Mon, Ryohei Sugahara, Jaeman Lee, Yutaka Kawaguchi and Takahiro Kusakabe, Analysis of the interactions between BRCA2 and RAD51 in silkworm, Bombyx mori, 平成21年日本分子生物学会本会, 2009.12.
77. Hiroaki Mon, Ryohei Sugahara, Jaeman Lee, Yutaka Kawaguchi and Takahiro Kusakabe, Analysis of the interactions between BRCA2 and RAD51 in silkworm, Bombyx mori, 平成21年日本分子生物学会本会, 2009.12.
78. Makiko Izumi , Hitoshi Mitsunobu , Hiroaki Mon , Kazuhiro Iiyama , Hiroyuki Jikuya, JaeMan Lee , Yutaka Kawaguchi , Takahiro Kusakabe, Analysis of Post-translational modifications of histones in Bombyx mori, 平成21年日本分子生物学会本会, 2009.12.
79. Shinji Ohkubo, Ryohei Sugahara, Hiroaki Mon, Masateru Takahashi, Tsuneyuki Tatsuke, Yosuke Taniguchi, Shigeki Sasaki, Jaeman Lee, Yutaka Kawaguchi and Takahiro Kusakabe, Analysis of DNA interstrand crosslink repair in silkworm, Bombyx mori , 平成21年日本分子生物学会本会, 2009.12.
80. Kokoro Shimada, Masateru Takahashi, Yoshiyuki Miyagawa, Kazuei Mita, Tsuneyuki Tatsuke, JaeMan Lee, Takahiro Kusakabe, Yutaka Kawaguchi, Cloning and characterization of p53 homolog in silkworm, Bombyx mori, 平成21年日本分子生物学会本会, 2009.12.
81. Kiyoko Miyata, Hitoshi Mitsunobu, Hiroaki Mon, JaeMan Lee, Yutaka Kawaguchi, Takahiro Kusakabe, Interaction between Tip60 and Histones in Bombyx mori, 平成21年日本分子生物学会本会, 2009.12.
82. Yuki Masaki, Tsuneyuki Tatsuke, Kosuke Sakashita, Shingo Yoshizue, JaeMan Lee, Yutaka Kawaguchi, Takahiro Kusakabe, The analysis of mechanism of the factors involved in RNAi in silkworm, 平成21年日本分子生物学会本会, 2009.12.
83. SunMee Hong, Hitoshi Mitsunobu, Jun Yamashita, Hideki Sezutsu, Toshiki Tamura, Hiroaki Mon, JaeMan Lee , Yutaka Kawaguchi , Takahiro Kusakabe, Characterization of Light Chain Homologue Ferritin and the Efficient Production on Silkworm Expressing Cytoplasmic Chaperones, 平成21年日本分子生物学会本会, 2009.12.
84. 門 宏明・李 在萬・日下部宜宏・河口 豊, カイコにおける相同組換え関連遺伝子の機能解析, 昆虫ワークショップ2009, 2009.09.
85. 大久保慎司・管原亮平・門 宏明・高橋将晃・李 在萬・日下部宜宏・河口 豊, カイコにおけるDNA鎖間架橋修復の解析, 昆虫ワークショップ2009, 2009.09.
86. 山下 隼・門 宏明・宮川世志幸・光延仁志・李 在萬・河口 豊・日下部宜宏, The interaction of BmHsp90 cochaperones with mammalian MAPKs and insect hormone receptors., 蚕糸学会本会(東京), 2009.03.
87. 光延仁志・竹野奈津美・門 宏明・李 在萬・小林 功・田村俊樹・小倉絵里・蒲池雄介・日下部宜宏・河口 豊, カイコにおけるヘテロクロマチン誘導による転写抑制, 蚕糸学会本会(東京), 2009.03.
88. 管原亮平・門宏明・大久保慎司・谷口陽祐・佐々木茂貴・李在萬・河口豊・日下部宜宏, カイコにおけるファンコニ経路因子FancI, D2複合体の解析, 蚕糸学会本会(東京), 2009.03.
89. 李 在萬・久保雄二・大畑 敬一・伴野 豊・河口 豊・日下部 宜宏, BmNPV高感受性カイコを用いた交配系統による効果的タンパク発現の試み(2), 蚕糸学会本会(東京), 2009.03.
90. 李 在萬・張平波・伴野 豊・河口 豊・日下部 宜宏, 高効率的組換えタンパク質発現用宿主としてのカイコ系統の開発(3), 蚕糸学会本会(名古屋), 2008.03.
特許出願・取得
特許出願件数  2件
特許登録件数  0件
学会活動
所属学会名
日本蚕糸学会
日本蚕糸学会九州支部会
学協会役員等への就任
2013.05~2016.05, 日本蚕糸学九州支部学会, 会計.
学会大会・会議・シンポジウム等における役割
2008.11.01~2016.05.18, 日本蚕糸学会九州支部会, 座長(Chairmanship).
2007.11, 日本蚕糸学会九州支部会, 座長(Chairmanship).
2005.11, 日本蚕糸学会九州支部会, 座長(Chairmanship).
学術論文等の審査
年度 外国語雑誌査読論文数 日本語雑誌査読論文数 国際会議録査読論文数 国内会議録査読論文数 合計
2019年度      
2018年度      
受賞
蚕糸学進歩賞(技術賞), 社団法人日本蚕糸学会(1930年創設), 2009.03.
蚕糸学進歩賞(技術賞), 社団法人日本蚕糸学会(1930年創設), 2008.03.
研究資金
科学研究費補助金の採択状況(文部科学省、日本学術振興会)
2018年度~2022年度, 基盤研究(B), 分担, 新規に同定された短い遺伝子にコードされるホルモン様ペプチドの機能.
2015年度~2018年度, 基盤研究(B), 代表, 昆虫工場におけるタンパク質糖鎖修飾の解析と改変.
2014年度~2015年度, 萌芽研究, 代表, 昆虫細胞における新規遺伝子導入技術の確立.
2011年度~2013年度, 基盤研究(C), 代表, 昆虫細胞におけるdsRNA応答機構の解析.
2009年度~2010年度, 萌芽研究, 分担, 昆虫分散型動原体染色体の謎.
2005年度~2006年度, 萌芽研究, 分担, 温泉ユスリカ由来耐熱タンパク質の解析.
2005年度~2007年度, 基盤研究(B), 分担, 昆虫における遺伝子ターゲティングの分子機構とその効率的利用.
競争的資金(受託研究を含む)の採択状況
2017年度~2018年度, 公益財団法人 柿原科学技術研究財団, 代表, 昆虫工場による豚用VLP型修飾多価 ワクチンの開発.
2008年度~2008年度, 独立行政法人 科学技術振興機構(JST), 代表, 高効率で安全な組換えウイルス増殖用カイコ細胞Bme21の無血清培養技術の開発.
2006年度~2010年度, 新技術・新分野創出のための基礎研究推進事業, 分担, 高効率物質生産系宿主としてのカイコのポストゲノム育種.
学内資金・基金等への採択状況
2017年度~2017年度, 大学発ベンチャー事業育成支援プログラム, 分担, 九大カイコバイオリソースを用いた人工細胞接着因子融合タンパク質の生産.
2016年度~2017年度, QRプログラム(わかばチャレンジ), 代表, 高機能ワクチンとしてのVLP修飾技術基盤の開発.
2006年度, 九州大学農学研究院若手教員支援事業, 分担, 病原細菌のDNA修復機構と宿主生体防御機構との相互作用.

九大関連コンテンツ

pure2017年10月2日から、「九州大学研究者情報」を補完するデータベースとして、Elsevier社の「Pure」による研究業績の公開を開始しました。
 
 
九州大学知的財産本部「九州大学Seeds集」