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Chemical Crosslinking of Tick-borne Encephalitis Virus and its Subunits

Institute of Virology, University of Vienna, A-1095 Vienna, Austria

Tick-borne encephalitis (TBE) virus was crosslinked by dimethylsuberimidate (DMS) and the cleavable dimethyl 3,3'-dithiobispropionimidate (DTBP). Analysis by SDS-PAGE revealed polymers of the virus core protein V₂ and the glycoprotein V₃ in continuously decreasing amounts. The formation of higher order complexes was not favoured over the formation of lower order complexes. This is consistent with an even distribution of V₃ molecules on the surface of the virion and of V₂ in the core. The formation of polymers was completely abolished by SDS, whereas crosslinking of TBE virus disrupted with a large excess of mild detergents (Triton X-100, octylglucoside, Na-deoxycholate) still yielded V₃ dimers but only negligible amounts of higher polymers. This indicates that in the presence of these detergents the basic subunit of the TBE virus envelope is composed of two V₃ molocules, probably associated with V₁. Using two-dimensional PAGE analysis of DTBP crosslinked complete virions or cores, no heterocomplexes between different virus proteins could be found which were small enough to penetrate a 5% gel. Crosslinking between V₃ molecules only and V₂ molecules only was therefore highly favoured over other reactions.

Received 29 June 1979; accepted 31 August 1979.