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Improved adenovirus type 5 vector-mediated transduction of resistant cells by piggybacking on coxsackie B-adenovirus receptor-pseudotyped baculovirus.

Journal article
Authors Ophélia Granio
Marine Porcherot
Stéphanie Corjon
Kuntida Kitidee
Petra Henning
Assia Eljaafari
Andrea Cimarelli
Leif Lindholm
Pierre Miossec
Pierre Boulanger
Saw-See Hong
Published in Journal of virology
Volume 83
Issue 12
Pages 6048-66
ISSN 1098-5514
Publication year 2009
Published at Institute of Biomedicine
Institute of Biomedicine, Department of Microbiology and Immunology
Pages 6048-66
Language en
Keywords Adenoviruses, Human, genetics, ultrastructure, Animals, Baculoviridae, genetics, ultrastructure, Cell Line, Female, Genetic Vectors, Green Fluorescent Proteins, genetics, Humans, Mice, Mice, Inbred BALB C, Mice, Nude, Receptors, Virus, genetics, Recombinant Fusion Proteins, genetics, Transduction, Genetic
Subject categories Microbiology in the medical area


Taking advantage of the wide tropism of baculoviruses (BVs), we constructed a recombinant BV (BV(CAR)) pseudotyped with human coxsackie B-adenovirus receptor (CAR), the high-affinity attachment receptor for adenovirus type 5 (Ad5), and used the strategy of piggybacking Ad5-green fluorescent protein (Ad5GFP) vector on BV(CAR) to transduce various cells refractory to Ad5 infection. We found that transduction of all cells tested, including human primary cells and cancer cell lines, was significantly improved using the BV(CAR)-Ad5GFP biviral complex compared to that obtained with Ad5GFP or BV(CAR)GFP alone. We determined the optimal conditions for the formation of the complex and found that a high level of BV(CAR)-Ad5GFP-mediated transduction occurred at relatively low adenovirus vector doses, compared with transduction by Ad5GFP alone. The increase in transduction was dependent on the direct coupling of BV(CAR) to Ad5GFP via CAR-fiber knob interaction, and the cell attachment of the BV(CAR)-Ad5GFP complex was mediated by the baculoviral envelope glycoprotein gp64. Analysis of the virus-cell binding reaction indicated that the presence of BV(CAR) in the complex provided kinetic benefits to Ad5GFP compared to the effects with Ad5GFP alone. The endocytic pathway of BV(CAR)-Ad5GFP did not require Ad5 penton base RGD-integrin interaction. Biodistribution of BV(CAR)-Ad5Luc complex in vivo was studied by intravenous administration to nude BALB/c mice and compared to Ad5Luc injected alone. No significant difference in viscerotropism was found between the two inocula, and the liver remained the preferred localization. In vitro, coagulation factor X drastically increased the Ad5GFP-mediated transduction of CAR-negative cells but had no effect on the efficiency of transduction by the BV(CAR)-Ad5GFP complex. Various situations in vitro or ex vivo in which our BV(CAR)-Ad5 duo could be advantageously used as gene transfer biviral vector are discussed.

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