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Graham Bottley,1
Lucy P. Beales,2
Richard A. Killington,1
David J. Rowlands,1 and
Tobias J. Tuthill1*
Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, The University of Leeds, Leeds LS2 9JT, United Kingdom,1 iQur Ltd., Faculty of Biological Sciences, The University of Leeds, Leeds LS2 9JT, United Kingdom2
Received 17 May 2007/ Accepted 21 January 2008
In common with all nonenveloped viruses, the mechanism of picornavirus membrane penetration during cell entry is poorly understood. The small, myristylated capsid protein VP4 has been implicated in this process. Here we show that recombinant VP4 of human rhinovirus 16 has the ability to associate with and induce membrane permeability in otherwise intact liposomes. This provides further evidence that VP4 plays a key role in picornavirus cell entry.
Published ahead of print on 6 February 2008.
Present address: Centre for Infectious Diseases, University of Edinburgh, Summerhall, Edinburgh EH9 1QH, United Kingdom.
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
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| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
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