Isolation of dimeric glycoprotein subunits from tick-borne encephalitis virus.
Crosslinking of tick-borne encephalitis virus with dimethylsuberimidate followed by SDS-PAGE analysis yielded polymers of the core protein V2 and the viral glycoprotein V3, both in continuously decreasing amounts. As the two structural entities of flaviviruses - cores and viral envelope - are apparently crosslinked independently from one another, we employed this property to study the action of different detergents at various concentrations on either the viral envelope or core. Triton X-100 and octylglucoside had no influence on the core but did dissociate the envelope into a V3-dimer. Centrifugation in density gradients containing these detergents yielded a 5-6S lipid-free hemagglutinating subunit which most probably represents a V3-dimer. In the presence of Triton X-100 this complex contains V1 in addition to V3.
D002499:Centrifugation, Density Gradient; D003840:Deoxycholic Acid / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology; D004120:Dimethyl Suberimidate; D004591:Electrophoresis, Polyacrylamide Gel; D004669:Encephalitis Viruses, Tick-Borne / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis / Q000302:isolation & purification*; D011092:Polyethylene Glycols / Q000494:pharmacology; D014764:Viral Proteins / Q000032:analysis / Q000302:isolation & purification*
D003902:Detergents; D006023:Glycoproteins; D014764:Viral Proteins; D003840:Deoxycholic Acid; D004120:Dimethyl Suberimidate; D011092:Polyethylene Glycols