Mimicking early events of virus infection: capillary electrophoretic analysis of virus attachment to receptor-decorated liposomes.

The attachment of human rhinovirus serotype 2 to an artificial cell membrane was followed by capillary electrophoresis. The cell membrane was mimicked by liposomes (average diameter of about 190 nm) containing a lipid with a nitrilotriacetic acid (NTA) group. This group, in the presence of Ni(2+) ions, served as anchor for the his(6)-tags of recombinant derivatives of the very-low-density lipoprotein (VLDL) receptor comprising either modules 1, 2, and 3 (V123) or five tandem copies of module 3 (V33333). We demonstrate by capillary electrophoresis with laser induced fluorescence detection of the liposomes that the minor receptor group rhinovirus HRV2 binds specifically to the receptor-decorated vesicles; the major receptor group rhinovirus HRV14, which uses a different receptor for cell binding, does not attach to the liposomes.