title: Intrinsic glycosylation potentials of insect cell cultures and insect larvae.
abstract: 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.
authors.affiliation: Boyce Thompson Institute for Plant Research, Ithaca, New York 14853, USA.
authors.forename: T R
authors.initials: TR
authors.lastname: Davis
authors.forename: H A
authors.initials: HA
authors.lastname: Wood
mesh_terms: 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*
chemical_list: D006023:Glycoproteins; D037102:Lectins; D011134:Polysaccharides; D011994:Recombinant Proteins; D000469:Alkaline Phosphatase