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Journal of Virology, June 2009, p. 6048-6066, Vol. 83, No. 12
0022-538X/09/$08.00+0     doi:10.1128/JVI.00012-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Improved Adenovirus Type 5 Vector-Mediated Transduction of Resistant Cells by Piggybacking on Coxsackie B-Adenovirus Receptor-Pseudotyped Baculovirus{triangledown}

Ophélia Granio,1,{dagger} Marine Porcherot,1,{dagger} Stéphanie Corjon,1 Kuntida Kitidee,1,2 Petra Henning,3 Assia Eljaafari,4 Andrea Cimarelli,5 Leif Lindholm,6 Pierre Miossec,4 Pierre Boulanger,1,7 and Saw-See Hong1*

Université Lyon I, Laboratoire de Virologie et Pathologie Humaine, CNRS FRE 3011, Faculté de Médecine Claude Bernard and IFR Laennec, 7, rue Guillaume Paradin, 69372 Lyon, France,1 Division of Clinical Immunology, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai, 50200 Thailand,2 Institute for Biomedicine, Department of Microbiology and Immunology, University of Göteborg, P.O. Box 435, SE 40530 Göteborg, Sweden,3 Department of Immunology and Rheumatology, Hôpital Edouard Herriot, 69437 Lyon, France,4 LaboRetro, Department of Human Virology, Ecole Normale Supérieure de Lyon, INSERM U 758, Université Lyon I, IFR128 BioSciences Lyon-Gerland, Lyon-Biopole, 46, Allée d'Italie, 69364 Lyon, France,5 Got-A-Gene AB, Östra Kyviksvägen 18, SE 42930 Kullavik, Sweden,6 Laboratoire de Virologie Médicale, Centre de Biologie Est, Hospices Civils de Lyon, 59, Boulevard Pinel, 69677 Bron, France7

Received 5 January 2009/ Accepted 27 March 2009

Taking advantage of the wide tropism of baculoviruses (BVs), we constructed a recombinant BV (BVCAR) 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 BVCAR 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 BVCAR-Ad5GFP biviral complex compared to that obtained with Ad5GFP or BVCARGFP alone. We determined the optimal conditions for the formation of the complex and found that a high level of BVCAR-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 BVCAR to Ad5GFP via CAR-fiber knob interaction, and the cell attachment of the BVCAR-Ad5GFP complex was mediated by the baculoviral envelope glycoprotein gp64. Analysis of the virus-cell binding reaction indicated that the presence of BVCAR in the complex provided kinetic benefits to Ad5GFP compared to the effects with Ad5GFP alone. The endocytic pathway of BVCAR-Ad5GFP did not require Ad5 penton base RGD-integrin interaction. Biodistribution of BVCAR-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 BVCAR-Ad5GFP complex. Various situations in vitro or ex vivo in which our BVCAR-Ad5 duo could be advantageously used as gene transfer biviral vector are discussed.

* Corresponding author. Mailing address: Laboratoire de Virologie et Pathologie Humaine, CNRS FRE 3011, Faculté de Médecine and IFR Laennec, 7, rue Guillaume Paradin, 69372 Lyon, France. Phone: (33) 4 7877 8621. Fax: (33) 4 7877 8751. E-mail: sawsee.hong{at}sante.univ-lyon1.fr

{triangledown} Published ahead of print on 8 April 2009.

{dagger} These authors contributed equally to this work.

Journal of Virology, June 2009, p. 6048-6066, Vol. 83, No. 12
0022-538X/09/$08.00+0     doi:10.1128/JVI.00012-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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