Generation of specificity-variant antibodies by alteration of carbohydrate in light chain of human monoclonal antibodies

Hirofumi Tachibana, Sanetaka Shirahata, Hiroki Murakami

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)

Abstract

A hybridoma line, C5TN, produced human monoclonal antibody of which light chain had N-linked carbohydrate chain within the variable region. Some molecular-weight variants of light chain of the antibody were produced by C5TN variants resistant to cytotoxic effect of concanavalin A. The variant antibodies significantly altered the original cross-reactivity with antigens or lost the ability of antigen binding. The variants variously trimmed their carbohydrate chains by glycosidases, showed the changed reactivity or acquired the ability to bind for antigens. The carbohydrate-deficient antibodies from tunicamycin-treated C5TN and the variant clones behaved in a similar manner on antigen-binding reactivity. Furthermore, comparison of antibodies of which light chains have carbohydrate chains sensitive and resistant to some glycosidases showed that carbohydrate chain in variable region of light chain can influence their reactivity with antigen.

Original languageEnglish
Pages (from-to)625-632
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume189
Issue number2
DOIs
Publication statusPublished - Dec 15 1992

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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