Summary
Tick-borne encephalitis virus was treated with pronase or thermolysin. The resulting particles were banded in sucrose gradients and analyzed for polypeptide composition. Both enzymes caused a reduction in particle density from 1.19 to 1.15–1.16 g/cm3. No loss of viral lipid or nucleic acid could be observed. SDS-polyacrylamidegel electrophoresis showed that only the core protein V2 was unchanged whereas the envelope proteins V3 and V1 had disappeared from their original positions in the PAGE profile. Instead a new peptide(s) with molecular weight of 4000–6000 was found in which hydrophobic amino-acids were enriched.
Crosslinking by dimethyl-3.3′-dithiobispropionimidate (DTBP) made the virus resistent to solubilization of the envelope proteins by TX-100. This could be interpreted by the formation of a dense envelope protein network around the nucleocapsid preventing its liberation by TX-100. Some data however indicate that direct crosslinking of at least one of the envelope proteins with the core cannot be excluded.
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Heinz, F.X., Kunz, C. Protease treatment and chemical crosslinking of a Flavivirus: Tick borne encephalitis virus. Archives of Virology 60, 207–216 (1979). https://doi.org/10.1007/BF01317492
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DOI: https://doi.org/10.1007/BF01317492