Abstract
Treatment of tick-borne encephalitis (TBE) virus with Triton X-100 (TX-100), octylglucoside (OG) or cetyltrimethylammonium bromide (CTAB) caused dissociation of the virus envelope into dimers or monomers of the glycoprotein V3. By centrifugation into detergent-free sucrose density gradients, these subunits reassociated and formed hemagglutinating homogeneous glycoprotein complexes sedimenting at 15-16, 16-18 and 11-12S after TX-100, OG and CTAB treatment, respectively. Glycoprotein complexes obtained after TX-100 solubilization contained less than 1% lipid and detergent by weight.