Email this article N-glycosylation profile of the protective chimeric antibody ch14D5a against tick-borne encephalitis virus
- Authors: Baykov I.K.1, Matveev A.L.1, Kondratov I.G.2, Tikunova N.V.1
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Affiliations:
- Institute of Chemical Biology and Fundamental Medicine, Siberian Branch
- Limnological Institute, Siberian Branch
- Issue: Vol 43, No 1 (2017)
- Pages: 71-75
- Section: Article
- URL: https://journals.rcsi.science/1068-1620/article/view/228415
- DOI: https://doi.org/10.1134/S1068162017010022
- ID: 228415
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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.
About the authors
I. K. Baykov
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch
Author for correspondence.
Email: ivan_baykov@mail.ru
Russian Federation, Novosibirsk, 630090
A. L. Matveev
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch
Email: ivan_baykov@mail.ru
Russian Federation, Novosibirsk, 630090
I. G. Kondratov
Limnological Institute, Siberian Branch
Email: ivan_baykov@mail.ru
Russian Federation, Irkutsk, 664033
N. V. Tikunova
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch
Email: ivan_baykov@mail.ru
Russian Federation, Novosibirsk, 630090
