Antigen binding of an ovomucoid-specific antibody is affected by a carbohydrate chain located on the light chain variable region

Yoshinori Fujimura, Hirofumi Tachibana, Nozomu Eto, Koji Yamada

研究成果: ジャーナルへの寄稿学術誌査読

20 被引用数 (Scopus)

抄録

We cloned the variable regions of heavy and light chain genes of an anti-ovomucoid monoclonal antibody (MAb-OM21) produced by the mouse hybridoma cell line OM21. DNA sequence analysis showed that the light chain of the MAb-OM21 has only one potential N-glycosylation consensus sequence in the complementarity determining region 2 of the light chain. To find whether carbohydrate chains are located on the light chain, we assayed for the size of the light chain, after treatment with N-glycosidase, by western blotting, and also detection of the carbohydrate chains on the light chain was done using the lectin blot assay. A N-linked carbohydrate chain has been shown to bind to the light chain. To clarify the role of this carbohydrate chain in the light chain, we produced carbohydrate variant antibodies by N-deglycosylation using glycosidase or by expressing the antibody from different host cells. The N-deglycosylated variant antibody has greater antigen binding, and the antibody produced from the different host cells showed a reduced antigen binding activity and acquired the ability to react to ovalbumin. These results suggest that antigen binding of the ovomucoid specific antibody MAb-OM21 can be affected by the carbohydrate chain on the light chain variable region.

本文言語英語
ページ(範囲)2298-2305
ページ数8
ジャーナルBioscience, Biotechnology and Biochemistry
64
11
DOI
出版ステータス出版済み - 2000

!!!All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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