6533b7dcfe1ef96bd1271f0b
RESEARCH PRODUCT
Improved display of synthetic IgG-binding domains on the baculovirus surface.
Reingard GrabherrKirsi OjalaIan M. JonesWolfgang ErnstChristian Oker-blomJohanna Koskisubject
0301 basic medicineCancer ResearchvirusesRecombinant Fusion Proteins030106 microbiologyGenetic VectorsGene deliveryBiologySpodopteraVesicular stomatitis Indiana virusViral vectorCell Line03 medical and health sciencesViral Envelope ProteinsViral entryCricetinaeAnimalsMembrane GlycoproteinsImmune SerafungiGenetic Therapybiology.organism_classificationMolecular biologyFusion proteinNucleopolyhedroviruses030104 developmental biologyOncologyIgG bindingVesicular stomatitis virusImmunoglobulin Gbiology.proteinExpression cassetteBinding Sites AntibodyRabbitsProtein ABaculoviridaedescription
Improved display of foreign protein moieties in combination with beneficial alteration of the viral surface properties should be of value for targeted and enhanced gene delivery. Here, we describe a vector based on Autographa californica multiple nucleopolyhedrovirus (AcMNPV) displaying synthetic IgG-binding domains (ZZ) of protein A fused to the transmembrane anchor of vesicular stomatitis virus (VSV) G protein. This display vector was equipped with a GFP/EGFP expression cassette enabling fluorescent detection in both insect and mammalian cells. The virus construct displayed the biologically active fusion protein efficiently and showed increased binding capacity to IgG. As the display is carried out using a membrane anchor of foreign origin, gp64 is left intact for virus entry, which may increase gene expression in the transduced mammalian cells. In addition, the viral vector can be targeted to any desired cell type via binding of ZZ domains when an appropriate IgG antibody is available.
year | journal | country | edition | language |
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2004-01-31 | Technology in cancer researchtreatment |