Secretion of the antibacterial recombinant protein enbocin.
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 enbocin proteins. Thus, bPDI gene fusion is a useful addition to the BEVS for the large-scale production of bioactive recombinant proteins.
Department of Agricultural Biology, National Institute of Agricultural Science and Technology, RDA, Suwon 441-100, Korea.
Tae Won
TW
Goo
Eun Young
EY
Yun
Sung Wan
SW
Kim
Kwang Ho
KH
Choi
Seok Woo
SW
Kang
Kisang
K
Kwon
Joung-Soon
JS
Choi
O-Yu
OY
Kwon
D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D016367:Baculoviridae / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000502:physiology; D019476:Insect Proteins / Q000378:metabolism*; D009036:Moths / Q000502:physiology*; D011994:Recombinant Proteins / Q000378:metabolism / Q000494:pharmacology; D017384:Sequence Deletion
D000900:Anti-Bacterial Agents; D019476:Insect Proteins; D011994:Recombinant Proteins; C112412:enbocin protein, Bombyx mori