Baculovirus infection does not alter N-glycosylation in Spodoptera frugiperda cells.
Spodoptera frugiperda cells are the standard host system for baculovirus-vector-mediated expression of recombinant glycoproteins. In an attempt to explore their ability to produce complex N-glycans containing terminal neuraminic acid, we tested both mock- and AcMNPV-infected SF9 cells. To elucidate the structures of the carbohydrate chains of cellular glycoproteins, radiolabeled oligosaccharides were liberated by treatment with endo-H and glycopeptidase F. When the endo-H resistant material was subjected to sequential degradation with exoglycosidases, only truncated carbohydrates with the structures Man3GlcNAc2 and Man3[Fuc]GlcNAc2 were found. There was no evidence for the presence of neuraminic acid and complex N-glycans. The results indicate that SF9 cells have only a limited capacity to process N-glycans. Infection with AcMNPV has no significant effect on glycosylation in these cells.
Kretzchmar
E
E
Institut für Virologie, Philipps-Universität, Marburg, Germany.
Geyer
R
R
Klenk
H D
HD
D000581:Amidohydrolases / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006031:Glycosylation; D006596:Hexosaminidases / Q000378:metabolism; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D009036:Moths; D009438:Neuraminic Acids / Q000032:analysis; D017924:Nucleopolyhedroviruses / Q000502:physiology*; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D011134:Polysaccharides / Q000096:biosynthesis* / Q000737:chemistry
D009438:Neuraminic Acids; D011134:Polysaccharides; D006596:Hexosaminidases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase