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Characterization of a Disulphide Bridge-stabilized Antigenic Domain of Tick-borne Encephalitis Virus Structural Glycoprotein

G. Winkler

Institute of Virology, University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria

Proteolytic digestion of purified whole tick-borne encephalitis virus or its isolated envelope glycoprotein (E) in the form of rosettes yields an M_r 9000 fragment that is resistant to further digestion and carries polyclonal and monoclonal antibody-defined antigenic determinants. In a denaturation/renaturation experiment it was demonstrated that the antigenic reactivity of this domain, which was lost upon reduction and carboxymethylation, could be regained if the reducing agent was dialysed out before carboxymethylation. By the use of [³⁵S]cysteine-labelled E protein and amino acid analysis it was confirmed that the reacquisition of antigenic reactivity in the renaturation experiment was associated with the reformation of disulphide bridges, which apparently confer structural stability to this part of the molecule. By the experiments performed we have identified an independently folding antigenically active domain of the E protein that is stabilized by disulphide bridges and has a strong tendency for renaturation.

Keywords: TBE virus, E protein, disulphide bridges

Present address: Department of Molecular Genetics and Microbiology, Robert Wood Johnson Medical School, UMDNJ, Piscataway, New Jersey 08854, U.S.A.

Received 16 October 1986; accepted 14 April 1987.

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