Intrinsic glycosylation potentials of insect cell cultures and insect larvae.
The glycosylation and subsequent processing of native and recombinant glycoproteins expressed in established insect cell lines and insect larvae were compared. The Spodoptera frugiperda (Sf21) and Trichoplusia ni (TN-368 and BTI-Tn-5B1-4) cell lines possessed several intrinsic glycoproteins that are modified with both N- and O-linked oligosaccharides. The N-linked oligosaccharides were identified as both the simple (high mannose) and complex (containing sialic acid) types. Similarly, the T. ni larvae also possessed intrinsic glycoproteins that were modified with O-linked and simple and complex N-linked oligosaccharides. Additionally, human placental, secreted alkaline phosphatase (SEAP) produced during replication of a recombinant baculovirus in T. ni larvae was modified with complex oligosaccharide having sialic acid linked alpha(2-6) to galactose.
Davis
T R
TR
Boyce Thompson Institute for Plant Research, Ithaca, New York 14853, USA.
Wood
H A
HA
D000469:Alkaline Phosphatase / Q000235:genetics / Q000378:metabolism; D000818:Animals; D016367:Baculoviridae / Q000378:metabolism; D002240:Carbohydrate Sequence; D002460:Cell Line; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D007814:Larva; D037102:Lectins / Q000378:metabolism; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000378:metabolism*; D018411:Spodoptera / Q000378:metabolism*
D006023:Glycoproteins; D037102:Lectins; D011134:Polysaccharides; D011994:Recombinant Proteins; D000469:Alkaline Phosphatase