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Glycobiology vol 5 no 8 pp. 813-822, 1995
© 1995

research-article

Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions

M.Robert Lifely2, Christine Hale, Susan Boyce, Michael J. Keen and Jenny Phillips1

Department of Cell Biology, Wellcome Research Laboratories Beckenham, BR3 3BS, UK
1Department of Pathology, University of Cambridge Cambridge, CB2 1QP, UK

2To whom correspondence should be addressed at: Department of Medicinal Chemistry, Wellcome Research Laboratories, Beckenham, BR3 3BS, UK

Received on August 2, 1995; revised on September 11, 1995; accepted on September 11, 1995

CAMPATH-1H (where CAMPATH is a trade mark of Well-come group companies), a humanized IgG antibody used in the therapy of lymphoma, leukaemia and rheumatoid arthritis, has been expressed in Chinese hamster ovary, Y0 myeloma and NS0 myeloma cell lines. These engineered cell lines were grown under different culture conditions, and the antibody isolated and purified. N-Linked oligosaccharides, on the CH2 heavy chain region of the antibody, were isolated and analysed by hydrazlnolysis, high-performance anion-exchange chromatography with pulsed amperometric detection, laser-desorption mass spectrometry and sequential exoglycosidase treatment Both the glycosylation pattern and the biological activity of CAMPATH-1H, as measured by antibody-dependent cell-mediated cytotoxicity, were markedly affected by the cell line used to express the antibody. It is concluded that glycosylation of the antibody may be important in the clinical outcome of therapy.

ADCC antibody CAMPATH glycosylation oligosac-charide


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