A gene encoding the dimeric form of single-chain antibody fragments (scFv) was designed on the basis of the artificial gene coding monomeric scFv to tick-borne encephalitis glycoprotein E. The sequence encoding histidine oligomer was added to 3'-ends of the genes encoding the monomeric and dimeric forms of scFv antibodies. Escherichia coli strains were constructed for the production of monomeric and dimeric antibodies. These antibodies were purified using Ni-NTA resin. The specificity of the purified monomeric and dimeric antibodies in the binding reaction with tick-borne encephalitis virus was shown by ELISA and Western-blot analysis. The identity of glycoprotein E epitope bound by monomeric and dimeric scFv and parental monoclonal antibodies E6B was confirmed by competitive immunoassay.