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Blood, 15 October 2004, Vol. 104, No. 8, pp. 2540-2542. Prepublished online as a Blood First Edition Paper on June 22, 2004; DOI 10.1182/blood-2004-05-1733. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-05-1733v1 104/8/2540    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Cragg, M. S. Articles by Illidge, T. M. Search for Related Content PubMed PubMed Citation Articles by Cragg, M. S. Articles by Illidge, T. M. Related Collections Immunobiology Neoplasia Immunotherapy Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  NEOPLASIA Brief report A new anti-idiotype antibody capable of binding rituximab on the surface of lymphoma cells Mark S. Cragg, Mike B. Bayne, Alison L. Tutt, Ruth R. French, Stephen Beers, Martin J. Glennie, and Timothy M. Illidge From the Tenovus Research Laboratory, Southampton, United Kingdom; Cancer Research UK (CRUK) Oncology, Cancer Sciences Division, School of Medicine, University General Hospital, Southampton, United Kingdom; and Genmab, Utrecht, The Netherlands. The chimeric anti-CD20 monoclonal antibody (mAb), rituximab, is an established part of the management of many non-Hodgkin lymphomas. The in vivo action of rituximab remains elusive, and this partially reflects a lack of highly specific reagents to detect rituximab binding at the cell surface. Here we report a new high-affinity mAb (MB2A4) with fine specificity for the idiotype of rituximab. It is able to detect rituximab in vitro, in the presence of high levels of human immunoglobulin G (IgG), in the serum of patients receiving rituximab therapy, and, surprisingly, when rituximab is bound to CD20 on the cell surface. We propose that the anti–idiotype (Id) binds to rituximab molecules bound univalently at the cell surface, facilitated by the relatively high off-rate of rituximab. This reagent provides new insights into the binding of rituximab at the cell surface and demonstrates a mode of binding that could be exploited for the surface detection of other mAbs with clinical and biologic applications. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. Gertner-Dardenne, C. Bonnafous, C. Bezombes, A.-H. Capietto, V. Scaglione, S. Ingoure, D. Cendron, E. Gross, J.-F. Lepage, A. Quillet-Mary, et al. Bromohydrin pyrophosphate enhances antibody-dependent cell-mediated cytotoxicity induced by therapeutic antibodies Blood, May 14, 2009; 113(20): 4875 - 4884. [Abstract] [Full Text] [PDF] T. M. Illidge, M. Bayne, N. S. Brown, S. Chilton, M. S. Cragg, M. J. Glennie, Y. Du, V. Lewington, J. Smart, J. Thom, et al. Phase 1/2 study of fractionated 131I-rituximab in low-grade B-cell lymphoma: the effect of prior rituximab dosing and tumor burden on subsequent radioimmunotherapy Blood, February 12, 2009; 113(7): 1412 - 1421. [Abstract] [Full Text] [PDF] C. A. Walshe, S. A. Beers, R. R. French, C. H. T. Chan, P. W. Johnson, G. K. Packham, M. J. Glennie, and M. S. Cragg Induction of Cytosolic Calcium Flux by CD20 Is Dependent upon B Cell Antigen Receptor Signaling J. Biol. Chem., June 20, 2008; 283(25): 16971 - 16984. [Abstract] [Full Text] [PDF] S.-Y. Wang, E. Racila, R. P. Taylor, and G. J. Weiner NK-cell activation and antibody-dependent cellular cytotoxicity induced by rituximab-coated target cells is inhibited by the C3b component of complement Blood, February 1, 2008; 111(3): 1456 - 1463. [Abstract] [Full Text] [PDF]

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