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Journal of Virology, May 2003, p. 5360-5369, Vol. 77, No. 9
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.9.5360-5369.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Human Rhinovirus Type 2 Is Internalized by Clathrin-Mediated Endocytosis

Luc Snyers, Hannes Zwickl, and Dieter Blaas*

Institute of Medical Biochemistry, University of Vienna, Vienna Biocenter, A-1030 Vienna, Austria

Received 18 October 2002/ Accepted 7 February 2003

Using several approaches, we investigated the importance of clathrin-mediated endocytosis in the uptake of human rhinovirus serotype 2 (HRV2). By means of confocal immunofluorescence microscopy, we show that K+ depletion strongly reduces HRV2 internalization. Viral uptake was also substantially reduced by extraction of cholesterol from the plasma membrane with methyl-ß-cyclodextrin, which can inhibit clathrin-mediated endocytosis. In accordance with these data, overexpression of dynamin K44A in HeLa cells prevented HRV2 internalization, as judged by confocal immunofluorescence microscopy, and strongly reduced infection. We also demonstrate that HRV2 bound to the surface of HeLa cells is localized in coated pits but not in caveolae. Finally, transient overexpression of the specific dominant-negative inhibitors of clathrin-mediated endocytosis, the SH3 domain of amphiphysin and the C-terminal domain of AP180, potently inhibited internalization of HRV2. Taken together, these results indicate that HRV2 uses clathrin-mediated endocytosis to infect cells.

* Corresponding author. Mailing address: Institute of Medical Biochemistry, University of Vienna, Vienna Biocenter, Dr. Bohr Gasse 9/3, A-1030 Vienna, Austria. Phone: 43 1 4277 61630. Fax: 43 1 4277 9616. E-mail: dieter.blaas{at}univie.ac.at.

Journal of Virology, May 2003, p. 5360-5369, Vol. 77, No. 9
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.9.5360-5369.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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