Capsid Protein VP4 of Human Rhinovirus Induces Membrane Permeability by the Formation of a Size-Selective Multimeric Pore
Figure 5
VP4 forms a multimeric complex.
A. VP4His was incubated in the presence of the membrane-mimetic detergent DHPC or liposomes, or mock-treated (−), resolved by native PAGE and visualised by silver staining. The position of bands shown by arrows indicates potential migration of VP4His into the gel. B. VP4 was incubated with (+) or without (−) liposomes and crosslinked by the addition of DSP at 0.5 mM (+) or 1 mM (++). Samples were resolved by non-reducing SDS-PAGE and detected by western blot using antisera to VP4. DTT was used in some samples to reverse the crosslinking prior to SDS-PAGE. Arrows indicate VP4 multimers. Molecular mass markers (in kilodaltons) are indicated on the left.