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Expression and characterization of a divalent chimeric anti-human CD3 single chain antibody.

作者信息

Ma S, Thompson J, Hu H, Neville D M

机构信息

Laboratory of Molecular Biology, National Institute of Mental Health, Bethesda, MD 20892-4034, USA.

出版信息

Scand J Immunol. 1996 Feb;43(2):134-9. doi: 10.1046/j.1365-3083.1996.d01-22.x.

DOI:10.1046/j.1365-3083.1996.d01-22.x
PMID:8633192
Abstract

Murine anti-CD3 monoclonal antibodies (MoAbs) are used in clinical practice for immunosuppression. However, there are two major drawbacks to this treatment: the associated cytokine release syndrome and human anti-mouse antibody response. To overcome these side-effects, the authors generated a chimeric anti-human CD3 single chain antibody, scUCHT1. It is an IgM variant of UCHT1, a mouse IgG1 MoAb directed against human CD3. scUCHT1 consists of the light and heavy variable chain binding domains of UCHT1 and a human IgM Fc region (CH2 to CH4). scUCHT1 was produced by COS-7 and SP2/0 transfectants, and mainly assembled in a dimeric form. It retained the binding specificity and affinity of the parental MoAb UCHT1. In contrast to UCHT1, scUCHT1 did not induce T-cell proliferation and cytokine release (TNF-alpha and IFN-gamma) in in vitro assays. These results suggest that the engineered chimeric anti-CD3 single chain antibody (scUCHT1) may be useful in clinical immunosuppressive treatment.

摘要

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