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N-glycosylation profile of the protective chimeric antibody ch14D5a against tick-borne encephalitis virus

Abstract

The glycosylation profile of the chimeric antibody ch14D5a against the tick-borne encephalitis virus has been analyzed. It has been found that the ch14D5a antibody is completely N-glycosylated at the asparagine 297 residue of both heavy chains, and the major glycoforms correspond supposedly to glycoforms G0F, G1F, and G2F, which are most typical for human immunoglobulins IgG and for antibodies secreted by CHO cells.

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Abbreviations

CHO:

Chinese hamster ovary

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Correspondence to I. K. Baykov.

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The paper is based on the materials of the “Chemical Biology 2016” conference; Novosibirsk, Russia, July 24–29, 2016.

Original Russian Text © I.K. Baykov, A.L. Matveev, I.G. Kondratov, N.V. Tikunova, 2017, published in Bioorganicheskaya Khimiya, 2017, Vol. 43, No. 1, pp. 83–87.

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Baykov, I.K., Matveev, A.L., Kondratov, I.G. et al. N-glycosylation profile of the protective chimeric antibody ch14D5a against tick-borne encephalitis virus. Russ J Bioorg Chem 43, 71–75 (2017). https://doi.org/10.1134/S1068162017010022

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  • DOI: https://doi.org/10.1134/S1068162017010022

Keywords

  • immunoglobulins
  • glycosylation
  • tick-borne encephalitis
  • mass spectrometry