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Modifying the insect cell N-glycosylation pathway with immediate early baculovirus expression vectors

Nature Biotechnologyvolume 14pages12881292 (1996) | Download Citation



The baculovirus-insect cell expression system is well-suited for recombinant glycoprotein production because baculovirus vectors can provide high levels of expression and insect cells can modify newly synthesized proteins in eucaryotic fashion. However, the N-glycosylation pathway of baculovirus-infected insect cells differs from the pathway found in higher eucaryotes, as indicated by the fact that glycoproteins produced in the baculovirus system typically lack complex biantennary N-linked oligosaccharide side chains containing penultimate galactose and terminal sialic acid residues. We recently developed a new type of baculovirus vector that can express foreign genes immediately after infection under the control of the viral ie 1 promoter. These immediate early baculovirus expression vectors can be used to modify the insect cell N-glycosylation pathway and produce a foreign glycoprotein with more extensively processed N-linked oligosaccharides. These vectors can also be used to study the influence of the late steps in N-linked oligosaccharide processing on glycoprotein function. Further development could lead to baculovirus-insect cell expression systems that can produce recombinant glycoproteins with complex biantennary N-linked oligosaccharides structurally identical to those produced by higher eucaryotes.

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    • Eric E. Finn

    Present address: Regional Primate Research Center, University of Washington, P.O. Box 357330, Seattle, WA, 98195

  1. Donald L. Jarvis: e-mail:


  1. Department of Entomology and Center for Advanced Invertebrate Molecular Sciences, Texas A&M University, College Station, TX, 77843

    • Donald L. Jarvis


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