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Updated: Jun 18, 2026

Purification of Biotinylated Cell Surface Proteins from Rhipicephalus microplus Epithelial Gut Cells
Published on: July 23, 2017
[Neutralizing single-chain antibodies against the tick-borne encephalitis virus]
Abstract:
A recombinant pSC13D6 plasmid DNA was constructed based on cDNA fragments of genes encoding variable domains of heavy and light chains of the MKA 13D6 monoclonal antibody against glycoprotein of the tick-borne encephalitis (TBE) virus. This plasmid provided expression in Escherichia coli cells of the sc13D6 single-chain antibody against the TBE virus. The produced antibodies could bind to the TBE virus, strain 205, and the TBE virus recombinant E protein. The affinity constant of purified sc13D6 was (3.0 +/- 0.2) x 10(7) M(-1) for the equilibrium state and (2.8 +/- 0.3) x 10(7) M(-1) in the case of antigen-antibody formation on the surface. The obtained single-chain antibody could inhibit the infection potency of the TBE virus on a monolayer of eukaryotic cells. The calculated IC50 value for sc13D6 was 16.7 microg/ml.
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