Title |
Recombinant fusion protein of cholera toxin B subunit with YVAD secreted by Lactobacillus caseiinhibits lipopolysaccharide-induced caspase-1 activation and subsequent IL-1 beta secretion in Caco-2 cells
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Published in |
BMC Biotechnology, May 2014
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DOI | 10.1186/1472-6750-14-38 |
Pubmed ID | |
Authors |
Yukihiro Hiramatsu, Masatatsu Yamamoto, Tomomitsu Satho, Keiichi Irie, Akiko Kai, Saori Uyeda, Yuki Fukumitsu, Akihisa Toda, Takeshi Miyata, Fumio Miake, Takeshi Arakawa, Nobuhiro Kashige |
Abstract |
Lactobacillus species are used as bacterial vectors to deliver functional peptides to the intestine because they are delivered live to the intestine, colonize the mucosal surface, and continue to produce the desired protein. Previously, we generated a recombinant Lactobacillus casei secreting the cholera toxin B subunit (CTB), which can translocate into intestinal epithelial cells (IECs) through GM1 ganglioside. Recombinant fusion proteins of CTB with functional peptides have been used as carriers for the delivery of these peptides to IECs because of the high cell permeation capacity of recombinant CTB (rCTB). However, there have been no reports of rCTB fused with peptides expressed or secreted by Lactobacillus species. In this study, we constructed L. casei secreting a recombinant fusion protein of CTB with YVAD (rCTB-YVAD). YVAD is a tetrapeptide (tyrosine-valine-alanine-aspartic acid) that specifically inhibits caspase-1, which catalyzes the production of interleukin (IL)-1β, an inflammatory cytokine, from its inactive precursor. Here, we examined whether rCTB-YVAD secreted by L. casei binds to GM1 ganglioside and inhibits caspase-1 activation in Caco-2 cells used as a model of IECs. |
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Student > Master | 4 | 18% |
Student > Doctoral Student | 3 | 14% |
Researcher | 2 | 9% |
Student > Bachelor | 1 | 5% |
Other | 2 | 9% |
Unknown | 5 | 23% |
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Biochemistry, Genetics and Molecular Biology | 4 | 18% |
Immunology and Microbiology | 4 | 18% |
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Engineering | 1 | 5% |
Other | 0 | 0% |
Unknown | 7 | 32% |