title: Recombinant VP4 of human rhinovirus induces permeability in model membranes.
abstract: 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.
authors.affiliation: Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, The University of Leeds, Leeds LS2 9JT, United Kingdom.
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Davis
authors.forename: Graham
authors.initials: G
authors.lastname: Bottley
authors.forename: Lucy P
authors.initials: LP
authors.lastname: Beales
authors.forename: Richard A
authors.initials: RA
authors.lastname: Killington
authors.forename: David J
authors.initials: DJ
authors.lastname: Rowlands
authors.forename: Tobias J
authors.initials: TJ
authors.lastname: Tuthill
mesh_terms: D036022:Capsid Proteins / Q000378:metabolism*; D006801:Humans; D008081:Liposomes / Q000378:metabolism; D008566:Membranes / Q000378:metabolism*; D010539:Permeability; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D012229:Rhinovirus / Q000502:physiology*; D053586:Virus Internalization
chemical_list: D036022:Capsid Proteins; D008081:Liposomes; D011994:Recombinant Proteins