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Journal of Virology, November 2000, p. 10639-10649, Vol. 74, No. 22
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Canine Adenovirus Type 2 Attachment and Internalization: Coxsackievirus-Adenovirus Receptor, Alternative Receptors, and an RGD-Independent Pathway

Claire Soudais,1 Sylvie Boutin,1 Saw See Hong,2 Miguel Chillon,1 Olivier Danos,1 Jeffrey M. Bergelson,3 Pierre Boulanger,2 and Eric J. Kremer1,*

Généthon III and CNRS URA 1923, Evry,1 and Laboratoire de Virologie & Pathogénèse Virale, CNRS UMR 5537, Lyon,2 France, and Division of Immunologic and Infectious Diseases, Children's Hospital of Philadelphia, Philadelphia, Pennsylvania3

Received 1 May 2000/Accepted 21 August 2000

The best-characterized receptors for adenoviruses (Ads) are the coxsackievirus-Ad receptor (CAR) and integrins alpha vbeta 5 and alpha vbeta 3, which facilitate entry. The alpha v integrins recognize an Arg-Gly-Asp (RGD) motif found in some extracellular matrix proteins and in the penton base in most human Ads. Using a canine adenovirus type 2 (CAV-2) vector, we found that CHO cells that express CAR but not wild-type CHO cells are susceptible to CAV-2 transduction. Cells expressing alpha Mbeta 2 integrins or major histocompatibility complex class I (MHC-I) molecules but which do not express CAR were not transduced. Binding assays showed that CAV-2 attaches to a recombinant soluble form of CAR and that Ad type 5 (Ad5) fiber, penton base, and an anti-CAR antibody partially blocked attachment. Using fluorescently labeled CAV-2 particles, we found that in some cells nonpermissive for transduction, inhibition was at the point of internalization and not attachment. The transduction efficiency of CAV-2, which lacks an RGD motif, surprisingly mimicked that of Ad5 when tested in cells selectively expressing alpha vbeta 5 and alpha vbeta 3 integrins. Our results demonstrate that CAV-2 transduction is augmented by CAR and possibly by alpha vbeta 5, though transduction can be CAR and alpha vbeta 3/5 independent but is alpha Mbeta 2, MHC-I, and RGD independent, demonstrating a transduction mechanism which is distinct from that of Ad2/5.

* Corresponding author. Mailing address: Généthon III/CNRS URA 1923, 1bis, rue de l'Internationale, 91002 Evry, France. Phone: 33 (0) 1-69-47-10-30. Fax: 33 (0) 1-69-47-28-38. E-mail: ekremer{at}genethon.fr.

Journal of Virology, November 2000, p. 10639-10649, Vol. 74, No. 22
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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