J. Virol. doi:10.1128/JVI.01070-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.
Recombinant VP4 of human rhinovirus induces permeability in model membranes
Matthew P. Davis,
Graham Bottley,
Lucy P. Beales,
Richard A. Killington,
David J. Rowlands,
and
Tobias J. Tuthill*
Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, The University of Leeds, Leeds LS2 9JT, United Kingdom; iQur Ltd, Faculty of Biological Sciences, The University of Leeds, Leeds LS2 9JT, United Kingdom
* To whom correspondence should be addressed. Email:
t.tuthill{at}leeds.ac.uk.
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Abstract |
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In common with all non-enveloped 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.