Recombinant full-size human antibody to Ebola virus

A full-size human antibody to Ebola virus was constructed by joining genes encoding the constant domains of the heavy and light chains of human immunoglobulin with the corresponding DNA fragments encoding variable domains of the single-chain antibody 4D1 specific to Ebola virus, which was chosen fro...

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Veröffentlicht in:Russian journal of bioorganic chemistry 2007-11, Vol.33 (6), p.554-561
Hauptverfasser: Shingarova, L. N., Tikunova, N. V., Yun, T. E., Chepurnov, A. A., Aliev, T. K., Batanova, T. A., Boldyreva, E. F., Nekrasova, O. V., Toporova, V. A., Panina, A. A., Kirpichnikov, M. P., Sandakhchiev, L. S.
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Sprache:eng
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Zusammenfassung:A full-size human antibody to Ebola virus was constructed by joining genes encoding the constant domains of the heavy and light chains of human immunoglobulin with the corresponding DNA fragments encoding variable domains of the single-chain antibody 4D1 specific to Ebola virus, which was chosen from a combinatorial phage display library of single-strand human antibodies. Two expression plasmids, pCH1 and pCL1, containing the artificial genes encoding the light and heavy chains of human immunoglobulin, respectively, were constructed. Their cotransfection into the human embryonic kidney cell line HEK293T provided the production of a full-size recombinant human antibody. The affinity constant for the antibody was estimated by solid-phase enzyme-linked immunoassay to be 7.7 x 10 super(7) plus or minus 1.5 x 10 super(7) M super(-1). Like the parent single-chain antibody 4D1, the resulting antibody bound the nucleoprotein of Ebola virus and did not interact with the proteins of Marburg virus.
ISSN:1068-1620
1573-9163
1608-330X
DOI:10.1134/S1068162007060040