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Viral membrane proteins: new targets, new strategies

Viral genomes encode small membrane proteins which are found to change the membrane permeability for ions and small molecules. For some of these proteins there function and the mechanism of function are well established. The hypothesis is that all channel forming proteins have to assemble in the lipid bilayer to form homo‐oligomers and functional channels or pores. Vpu from HIV‐1, an 81 amino acid integral membrane protein, is taken to analyse assembly and channel characteristics in a combined computational and experimental (bilayer recordings) approach. Channel characteristics of Vpu are similar to those of a peptide corresponding to the membrane spanning domain. Therefore peptides and peptide mutants of Vpu are used. The experimental data in combination with computational models show a week cation selective channel suggesting a channel/pore dualism. Preliminary experimental data of Vpu‐blocking with cyclohexamethylene amiloride show altered channel kinetics.