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Blood, 15 September 2004, Vol. 104, No. 6, pp. 1793-1800.
Prepublished online as a Blood First Edition Paper on June 1, 2004; DOI 10.1182/blood-2004-01-0039.
 Previous Article | Table of Contents | Next Article 
IMMUNOBIOLOGY
Characterization of new human CD20 monoclonal antibodies with potent cytolytic activity against non-Hodgkin lymphomas
Jessica L. Teeling,
Ruth R. French,
Mark S. Cragg,
Jeroen van den Brakel,
Marielle Pluyter,
Haichun Huang,
Claude Chan,
Paul W. H. I. Parren,
C. Erik Hack,
Michael Dechant,
Thomas Valerius,
Jan G. J. van de Winkel, and
Martin J. Glennie
From Genmab, Utrecht, the Netherlands; Tenovus Research Laboratory, Cancer Sciences Division, School of Medicine, University General Hospital, Southampton, United Kingdom; the Department of Immunotherapy Laboratory, Department of Immunology, Universitair Medisch Centrum (UMC), Utrecht, the Netherlands; Medarex, Princeton, NJ; Sanquin Research at Centraal Laboratorium Bloedtransfusie (CLB), Vrije Universiteit (VU) University Medical Center, Amsterdam, the Netherlands; and the Department of Medicine I, University Schleswig-Holstein, Campus Kiel, Germany.
Despite the rapid and widespread integration of chimeric CD20 monoclonal antibody (mAb), rituximab, into the management of non-Hodgkin lymphoma, its efficacy remains variable and often modest when used as a single agent. To develop more potent reagents, human immunoglobulin transgenic mice were used to generate a panel of immunoglobulin G1 (IgG1) CD20 mAbs. All reagents bound strongly to CD20+ cells and recruited mononuclear cells for the lysis of malignant B cells. However, 2 mAbs, 2F2 and 7D8, were exceptionally active in complement-dependent cytotoxicity (CDC), being able to lyse a range of rituximab-resistant targets, such as CD20-low chronic lymphocytic leukemia (CLL), in the presence of human plasma or unfractionated blood. Further analysis showed that 2F2 and 7D8, like rituximab, redistributed CD20 into Triton X-100-insoluble regions of the plasma membrane, but that they had markedly slower off-rates. To determine whether off-rate influenced CDC, a non-complement activating F(ab')2 antihuman reagent was used. This reagent markedly slowed the off-rate of rituximab and increased its CDC activity to that of 2F2 and 7D8. Thus, with increasing evidence that mAb therapeutic activity in vivo depends on complement activation, these new CD20 reagents with their slow off-rates and increased potency in CDC hold considerable promise for improved clinical activity. (Blood. 2004;104:1793-1800)
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