pp 1-22 | Cite as

Glycobiotechnology of the Insect Cell-Baculovirus Expression System Technology

  • Laura A. Palomares
  • Indresh K. Srivastava
  • Octavio T. Ramírez
  • Manon M. J. CoxEmail author
Part of the Advances in Biochemical Engineering/Biotechnology book series


The insect cell-baculovirus expression system technology (BEST) has a prominent role in producing recombinant proteins to be used as research and diagnostic reagents and vaccines. The glycosylation profile of proteins produced by the BEST is composed predominantly of terminal mannose glycans, and, in Trichoplusia ni cell lines, core α3 fucosylation, a profile different to that in mammals. Insects contain all the enzymatic activities needed for complex N- and O-glycosylation and sialylation, although few reports of complex glycosylation and sialylation by the BEST exist. The insect cell line and culture conditions determine the glycosylation profile of proteins produced by the BEST. The promoter used, dissolved oxygen tension, presence of sugar precursors, bovine serum or hemolymph, temperature, and the time of harvest all influence glycosylation, although more research is needed. The lack of activity of glycosylation enzymes possibly results from the transcription regulation and stress imposed by baculovirus infection. To solve this limitation, the glycosylation pathway of insect cells has been engineered to produce complex sialylated glycans and to eliminate α3 fucosylation, either by generating transgenic cell lines or by using baculovirus vectors. These strategies have been successful. Complex glycosylation, sialylation, and inhibition of α3 fucosylation have been achieved, although the majority of glycans still have terminal mannose residues. The implication of insect glycosylation in the proteins produced by the BEST is discussed.

Graphical Abstract


Baculovirus Cell engineering Glycobiotechnology Glycosylation Insect cells Recombinant protein 



Baculovirus expression system technology


Chinese hamster ovary


Carbohydrate sulfotransferase 2


Sialic acid synthetase


Dissolved oxygen tension


Recombinant equine luteinizing hormone/chorionic gonadotropin


Endoplasmic reticulum


Fetal bovine serum


Fused lobes protein






α-1,3 Fucosyltransferase






Gal-3-O-sulfotransferase 2










GlcNAc transferase


Hours postinfection








Baculovirus basic protein promoter


Not detected


N-Acetylneuraminic acid


Not reported


Rat purple acid phosphatase


Recombinant influenza hemagglutinin


Recombinant lutropin receptor ectodomain


Guanosine-5′-diphospho (GDP)4-dehydro-6-deoxy-d-mannose reductase


Sialic acid 9-phosphate synthase


Secreted human alkaline phosphatase




Tissue plasminogen activator


β subunit of human chorionic gonadotropin



Research performed thanks to the support by UNAM-DGAPA-PAPIIT IT-200315. Technical assistance from Luis Alberto Diaz is acknowledged.


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Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  • Laura A. Palomares
    • 1
  • Indresh K. Srivastava
    • 2
  • Octavio T. Ramírez
    • 1
  • Manon M. J. Cox
    • 2
    Email author
  1. 1.Instituto de Biotecnología, Universidad Nacional Autónoma de MéxicoCuernavacaMexico
  2. 2.Protein Sciences Corporation, A Sanofi CompanyMeridenUSA

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