Bombyx mori protein disulfide isomerase enhances the production of nuecin, an antibacterial protein.
The insect baculovirus expression vector system (BEVS) is useful for producing biologically active recombinant proteins. However, the overexpressions of foreign 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 proteins. Thus, we conclude that bPDI gene fusion is a useful addition to BEVS for the large-scale production of bioactive recombinant proteins.
Department of Anatomy, College of Medicine, Chungnam National University, Daejon, Korea.
Tae Won
TW
Goo
Eun Young
EY
Yun
Sung Wan
SW
Kim
Kwang Ho
KH
Choi
Seok Woo
SW
Kang
Kisang
K
Kwon
Kweon
K
Yu
O-Yu
OY
Kwon
D000818:Animals; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D016367:Baculoviridae / Q000235:genetics; D012831:Bombyx / Q000201:enzymology* / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D005822:Genetic Vectors / Q000235:genetics; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism*; D008957:Models, Genetic; D019704:Protein Disulfide-Isomerases / Q000235:genetics / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D019476:Insect Proteins; C532270:nuecin protein, Bombyx mori; D019704:Protein Disulfide-Isomerases