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 V and the glycoprotein V 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 V molecules on the surface of the virion and of V 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 V 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 V molocules, probably associated with V. 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 V molecules only and V molecules only was therefore highly favoured over other reactions.


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