The baculovirus-insect cell expression system is well-suited for recom
binant glycoprotein production because baculovirus vectors can provide
high levels of expression and insect cells can modify newly synthesiz
ed proteins in eucaryotic fashion. However, the N-glycosylation pathwa
y of baculovirus-infected insect cells differs from the pathway found
in higher eucaryotes, as indicated by the fact that glycoproteins prod
uced in the baculovirus system typically lack complex biantennary N-li
nked oligosaccharide side chains containing penultimate galactose and
terminal sialic acid residues. We recently developed a new type of bac
ulovirus vector that cart express foreign genes immediately after infe
ction under the control of the viral ie1 promoter. These immediate ear
ly baculovirus expression vectors can be used to modify the insect cel
l N-glycosylation pathway and produce a foreign glycoprotein with more
extensively processed N-linked oligosaccharides, These vectors can al
so be used to study the influence of the late steps in N-linked oligos
accharide processing on glycoprotein function. Further development cou
ld lead to baculovirus-insect cell expression systems that can produce
recombinant glycoproteins with complex biantennary N-linked oligosacc
harides structurally identical to those produced by higher eucaryotes.