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.
Bilek
Gerhard
G
Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria.
Kremser
Leopold
L
Wruss
Jürgen
J
Blaas
Dieter
D
Kenndler
Ernst
E
D002462:Cell Membrane / Q000382:microbiology; D019075:Electrophoresis, Capillary / Q000295:instrumentation / Q000379:methods*; D006801:Humans; D008081:Liposomes / Q000032:analysis*; D008567:Membranes, Artificial; D010850:Picornaviridae Infections; D011973:Receptors, LDL / Q000032:analysis*; D012229:Rhinovirus / Q000737:chemistry*; D012680:Sensitivity and Specificity; D013997:Time Factors
D008081:Liposomes; D008567:Membranes, Artificial; D011973:Receptors, LDL