Baculoviral display of the green fluorescent protein and rubella virus envelope proteins

David Mottershead, Inge van der Linden, Carl-Henrik von Bonsdorff, Kari Keinänen, Christian Oker-Blom (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

68 Citations (Scopus)

Abstract

The ability to display heterologous proteins and peptides on the surface of different types of bacteriophage has proven extremely useful in protein structure/function studies. To display such proteins in a eucaryotic environment, we have produced a vector allowing for fusion of proteins to the amino-terminus of theAutographa californicanuclear polyhedrosis virus (AcNPV) major envelope glycoprotein, gp64. Such fusion proteins incorporate into the baculoviral virion and display the FLAG epitope tag. We have further produced recombinant baculoviruses displaying the green fluorescent protein (GFP) and the rubella virus envelope proteins, E1 and E2. The incorporation of the GFPgp64, E1gp64, and E2gp64 fusion proteins into the baculovirus particle was demonstrated by western blot analysis of purified budded virus. This is the first report of the display of the GFP protein or the individual rubella virus spike proteins on the surface of an enveloped virus. Such a eucaryotic viral display system may be useful for the display of proteins dependent on glycosylation for activity and for targeting of recombinant baculoviruses to novel host cell types as a gene transfer vehicle.

Original languageEnglish
Pages (from-to)717 - 722
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume238
Issue number3
DOIs
Publication statusPublished - 1997
MoE publication typeA1 Journal article-refereed

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Viral Envelope Proteins
Rubella virus
Green Fluorescent Proteins
Display devices
Viruses
Baculoviridae
Proteins
Fusion reactions
Glycosylation
Gene transfer
Bacteriophages
Virion
Epitopes
Glycoproteins
Membrane Proteins
Western Blotting
Peptides

Cite this

Mottershead, David ; Linden, Inge van der ; Bonsdorff, Carl-Henrik von ; Keinänen, Kari ; Oker-Blom, Christian. / Baculoviral display of the green fluorescent protein and rubella virus envelope proteins. In: Biochemical and Biophysical Research Communications. 1997 ; Vol. 238, No. 3. pp. 717 - 722.
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abstract = "The ability to display heterologous proteins and peptides on the surface of different types of bacteriophage has proven extremely useful in protein structure/function studies. To display such proteins in a eucaryotic environment, we have produced a vector allowing for fusion of proteins to the amino-terminus of theAutographa californicanuclear polyhedrosis virus (AcNPV) major envelope glycoprotein, gp64. Such fusion proteins incorporate into the baculoviral virion and display the FLAG epitope tag. We have further produced recombinant baculoviruses displaying the green fluorescent protein (GFP) and the rubella virus envelope proteins, E1 and E2. The incorporation of the GFPgp64, E1gp64, and E2gp64 fusion proteins into the baculovirus particle was demonstrated by western blot analysis of purified budded virus. This is the first report of the display of the GFP protein or the individual rubella virus spike proteins on the surface of an enveloped virus. Such a eucaryotic viral display system may be useful for the display of proteins dependent on glycosylation for activity and for targeting of recombinant baculoviruses to novel host cell types as a gene transfer vehicle.",
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Mottershead, D, Linden, IVD, Bonsdorff, C-HV, Keinänen, K & Oker-Blom, C 1997, 'Baculoviral display of the green fluorescent protein and rubella virus envelope proteins', Biochemical and Biophysical Research Communications, vol. 238, no. 3, pp. 717 - 722. https://doi.org/10.1006/bbrc.1997.7372

Baculoviral display of the green fluorescent protein and rubella virus envelope proteins. / Mottershead, David; Linden, Inge van der; Bonsdorff, Carl-Henrik von; Keinänen, Kari; Oker-Blom, Christian (Corresponding Author).

In: Biochemical and Biophysical Research Communications, Vol. 238, No. 3, 1997, p. 717 - 722.

Research output: Contribution to journalArticleScientificpeer-review

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