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PCR cloning of the antigen binding domains of an MCF7-specific monoclonal antibody

Adoptive immunotherapy for cancer, using tumor-infiltrating lymphocytes (TIL), is often limited by the lack of specificity of these TIL after expansion in vitro. To circumvent this problem we constructed a chimeric T-cell receptor (cTCR) in which the antigen binding domains of the TCR are replaced b...

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Bibliographic Details
Published in:Immunogenetics (New York) 1994-07, Vol.40 (3), p.245-245
Main Authors: MOTMANS, K, VANDEVYVER, C, RAUS, J
Format: Article
Language:English
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Summary:Adoptive immunotherapy for cancer, using tumor-infiltrating lymphocytes (TIL), is often limited by the lack of specificity of these TIL after expansion in vitro. To circumvent this problem we constructed a chimeric T-cell receptor (cTCR) in which the antigen binding domains of the TCR are replaced by those of a monoclonal antibody that recognizes a tumor-associated antigen. T cells expressing a cTCR recognize their antigen in a major histocompatibility complex (MHC)-unrestricted manner. MCF7 (human breast Carcinoma cell line)-specific monoclonal antibodies were obtained by fusing spleen cells from immunized mice with SP2/0 myeloma cells. One of the antibodies, 11F9 (subtype: IgG2a), revealed a high specificity for infiltrating ductal adenocarcinomas and little reactivity with normal epithelial tissues. In vivo studies in nude mice bearing an MCF7-induced tumor showed a significant migration of the 11F9 antibody to the tumor tissue.
ISSN:0093-7711
1432-1211
DOI:10.1007/BF00167089