Recombinant VP4 of human rhinovirus induces permeability in model membranes.
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.
Davis
Matthew P
MP
Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, The University of Leeds, Leeds LS2 9JT, United Kingdom.
Bottley
Graham
G
Beales
Lucy P
LP
Killington
Richard A
RA
Rowlands
David J
DJ
Tuthill
Tobias J
TJ
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
D036022:Capsid Proteins; D008081:Liposomes; D011994:Recombinant Proteins