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Goo, Tae-Won,Kim, Seong-Wan,Choi, Kwang-Ho,Kim, Seong-Ryul,Kang, Seok-Woo,Park, Seung-Won,Yun, Eun-Young Korean Society of Sericultural Science 2013 International Journal of Industrial Entomology Vol.26 No.2
The insect baculovirus expression vector system (BEVS) is useful for producing biologically active recombinant proteins. However, the overexpression of heterologous proteins using this system often results in misfolded proteins and the formation of protein aggregates. To overcome this limitation, we developed a versatile baculovirus expression and secretion system using Bombyx mori protein disulfide isomerase (bPDI) as a fusion partner. bPDI gene fusion was found to improve the secretions and antibacterial activities of recombinant nuecin and enbocin proteins. Thus, we conclude that bPDI gene fusion is a useful addition to BEVS for the large-scale production of bioactive recombinant proteins.
( Tae Won Goo ),( Seong Wan Kim ),( Kwang Ho Choi ),( Seong Ryul Kim ),( Seok Woo Kang ),( Seung Won Park ),( Eun Young Yun ) 한국잠사학회 2013 International Journal of Industrial Entomology Vol.26 No.2
The insect baculovirus expression vector system (BEVS) is useful for producing biologically active recombinant proteins. However, the overexpression of heterologous proteins using this system often results in misfolded proteins and the formation of protein aggregates. To overcome this limitation, we developed a versatile baculovirus expression and secretion system using Bombyx mori protein disulfide isomerase (bPDI) as a fusion partner. bPDI gene fusion was found to improve the secretions and antibacterial activities of recombinant nuecin and enbocin proteins. Thus, we conclude that bPDI gene fusion is a useful addition to BEVS for the large-scale production of bioactive recombinant proteins.
A Strong Transcription Activity of the Bombyx mori Elongation Factor 1α Promoter
Goo, Tae-Won,Kim, Sung-Wan,Kim, Seong-Ryul,Park, Seung-Won,Kang, Seok-Woo,Choi, Kwang-Ho,Yun, Eun-Young Korean Society of Sericultural Science 2012 International Journal of Industrial Entomology Vol.24 No.2
We previously isolated 9 clones that show stronger signal compared to B. mori cytoplasmic actin gene (BmA3) by using a dot blot hybridization. In this study, we focused on one clone among these clones which has high amino acid homology with elongation factor ${\alpha}$ gene of B. mori. This clone, named $bEF1{\alpha}$ (B. mori elongation factor ${\alpha}$) was ubiquitously expressed in all tissues and developmental stage of B. mori. As result of promoter assay using dual luciferase assay system, we found the highest transcription activity region (-702/+38) in the 5'-flanking region of $bEF1{\alpha}$ gene, which has about 20 fold more intensive promoter activity than BmA3 promoter. Moreover, the $bEF1{\alpha}$ promoter was normally regulated in Bm5, Sf9, and S2 cells. Therefore, we suggest that $bEF1{\alpha}$ promoter may be used more powerful and effectively for transgene expression in various insects containing B. mori as a universal promoter.
Expression of the cyan fluorescent protein in fibroin H-chain of transgenic silkworm
( Tae-won Goo ),( Kwang-ho Choi ),( Seong-ryul Kim ),( Seung Won Park ),( Seong-wan Kim ) 한국잠사학회 2017 International Journal of Industrial Entomology Vol.34 No.1
We constructed the fibroin H-chain expression system to produce enhanced cyan fluorescent proteins (ECFP) in transgenic silkworm cocoon. Fluorescent cocoon could be made by fusing ECFP cDNA to the heavy chain gene and injecting it into a silkworm. The ECFP fusion protein, each with N- and C-terminal sequences of the fibroin H-chain, was designed to be secreted into the lumen of the posterior silk glands. The expression of the ECFP/H-chain fusion gene was regulated by the fibroin H-chain promoter. The use of the 3xP3-driven EGFP cDNA as a marker allowed us to rapidly distinguish transgenic silkworms. The EGFP fluorescence became visible in the ocelli and in the central and peripheral nervous system on the seventh day of embryonic development. A mixture of the donor and helper vector was micro-injected into 1,020 Kumokjam, bivoltin silkworm eggs. We obtained 6 broods. The cocoon was displayed strong blue fluorescence, proving that the fusion protein was present in the cocoon. Accordingly, we suggest that the ECFP fluorescence silk will enable the production of novel biomaterial based on the transgenic silk. ⓒ 2017 The Korean Society of Sericultural Sciences Int. J. Indust. Entomol. 34(1), 11-15 (2017)
Goo, Tae-Won,Yun, Eun-Young,Kim, Sung-Wan,Park, Kwang-Ho,Hwang, Jae-Sam,Kwon, O-Yu,Kang, Seok-Woo Korean Society of Sericultural Science 2003 International Journal of Industrial Entomology Vol.7 No.2
Protein disulfide isomerase (PDI) found in the endoplasmic reticulum (ER) catalyzes disulfide bond exchange and assists in protein folding of newly synthesized proteins. PDI also functions as a molecular chaperone and has been found to be associated with proteins in the ER. In addition, PDI functions as a subunit of two more complex enzyme systems: the prolyl-4-hydroxylase and the triacylglycerol transfer proteins. A cDNA that encodes protein disulfide isomerase was previously isolated from Bombyx mori (bPDI), in which open reading frame of 494 amino acids contained two PDI-typical thioredoxin active site of WCGHCK and an ER retention signal of the KDEL motif at its C-terminal, and we report its functional characterization here. This putative bPDI cDNA is expressed in insect Sf9 cells as a recombinant proteins using baculovirus expression vector system. The bPDI recombinant proteins are successfully recognized by antirat PDI antibody, and shown to be biologically active in vitro by mediating the oxidative refolding of reduced and scrambled RNase. This suggests that bPDI may play an important role in protein folding mechanism of insects.
Bombyx mori Protein Disulfide Isomerase Enhances the Production of Nuecin, an Antibacterial Protein
Tae Won Goo,Eun Young Yun,Sung Wan Kim,Kwang Ho Choi,Min Uk Kang,O-Yu Kwon,Seok Woo Kang 한국응용곤충학회 2008 한국응용곤충학회 학술대회논문집 Vol.2008 No.05
The insect baculovirus expression vector system (BEVS) is useful for the production of biologically active recombinant proteins. However, the overexpression of foreign proteins in this system often results in misfolded proteins and the formation of protein aggregates. To overcome this limitation, we have developed a versatile baculovirus expression and secretion system using the Bombyx mori protein disulfide isomerase (bPDI) as a fusion partner. bPDI gene fusion improved the secretion and antibacterial activity of recombinant nuecin proteins. Thus, bPDI gene fusion is a useful addition to the BEVS for the large-scale production of bioactive recombinant proteins.
A Bombyx mori Transcription Factor, ATFC Binds Directly to the UPRE of Molecular Chaperones
Goo, Tae-Won,Yun, Eun-Young,Kim, Sung-Wan,Park, Kwang-Ho,Hwang, Jae-Sam,Kwon, O-Yu,Kang, Seok-Woo Korean Society of Sericultural Science 2003 International Journal of Industrial Entomology Vol.7 No.2
Cells respond to an accumulation of unfolded proteins in the endoplasmic reticulum (ER) by increasing transcription of genes encoding molecular chaperones and folding enzymes. The information is transmitted from the ER lumen to the nucleus by intracellular signaling pathway, called the unfolded protein response (UPR). In Saccharomyces cerevisiae, such induction is mediated by the cis-acting unfolded response element (UPRE) which has been thought to be recognized by Hac1p transcription factor. We cloned the ATFC gene showing similarity with Hac1p, and then examined to determine whether ATFC gene product specifically binds to UPRE by electrophoretic mobility shift assays. ATFC gene product displayed appreciable binding ${to ^{32}}P-labelled$ UPRE. Therefore, we concluded that ATFC represents a major component of the putative transcription factor responsible for the UPR leading to the induction of ER-localized stress proteins.