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Recombinant Baculovirus Vectors Expressing Glutathione–S–Transferase Fusion Proteins

Bio/Technology volume 11, pages 933–936 (1993)Cite this article

Abstract

Recombinant baculoviruses are a popular means of producing heterologous protein in eukaryotic cells. Purification of recombinant proteins away from the insect cell background can, however, remain an obstacle for many developments. Recently, prokaryotic fusion protein expression systems have been developed allowing single-step purification of the heterologous protein and specific proteolytic cleavage of the affinity tag moiety from the desired antigen. Here we report the introduction of these attributes to the baculovirus system. “Baculo-GEX” vectors enable baculovirus production of fusion proteins with the above advantages, but in a eukaryotic post-translational processing environment. Glutathione-S-transferase (GST) fusions are stable cytoplasmic proteins in insect cells and may therefore be released by sonication alone, avoiding the solubility problems and detergent requirements of bacterial systems. Thus large amounts of authentic antigen may be purified in a single, non-denaturing step.

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Author notes

  1. Jeremy B. M. Jowett

    Present address: School of Medicine, Division of Hematology-Oncology, University of California, Los Angeles, CA, 90024–1678

  2. Anthony H. Davies

    Present address: School of Medicine, Department of Pathology, University of California, San Francisco, CA, 94143–0506

  3. Anthony H. Davies: Corresponding Author.

Authors and Affiliations

  1. Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford, OX1 3SR, UK

    Anthony H. Davies & Ian M. Jones

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  1. Anthony H. Davies
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  2. Jeremy B. M. Jowett
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  3. Ian M. Jones
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Davies, A., Jowett, J. & Jones, I. Recombinant Baculovirus Vectors Expressing Glutathione–S–Transferase Fusion Proteins. Nat Biotechnol 11, 933–936 (1993). https://doi.org/10.1038/nbt0893-933

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