Galatosylation and sialylation of mammalian glycoproteins produced by baculovirus-madiated gene expression in insect cells.
The baculovirus expression vector system (BEVS) is used extensively for the production of proteins from exogenous cDNAs. However, BEVS is not ideal for pharmaceutical production of glycoproteins owing to the properties of the N-glycans in the expressed products and that insect cells lack several of the enzymes required for mammalian-type N-glycan synthesis. This study describes the effective mammalian-like production of glycoproteins, such as beta-1,4-galactosyltransferase and alpha-2,6-sialyltransferase, in the insect cell line Sf9.
Yun
Eun-Young
EY
Department of Agricultural Biology, National Institute of Agricultural Science and Technology, 441-100, RDA, Suwon, Korea.
Goo
Tae-Won
TW
Kim
Sung-Wan
SW
Choi
Kwang-Ho
KH
Hwang
Jae-Sam
JS
Kang
Seok-Woo
SW
Kwon
O-Yu
OY
D000818:Animals; D016367:Baculoviridae; D006031:Glycosylation; D006801:Humans; D046188:Protein Modification, Translational / Q000235:genetics*; D051381:Rats; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics; D012799:Sialyltransferases / Q000096:biosynthesis* / Q000235:genetics; D018411:Spodoptera; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D011994:Recombinant Proteins; D012799:Sialyltransferases; C029156:N-acetyllactosaminide alpha-2,3-sialyltransferase; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase