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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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Published in: | Immunogenetics (New York) 1994-07, Vol.40 (3), p.245-245 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
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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. |
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ISSN: | 0093-7711 1432-1211 |
DOI: | 10.1007/BF00167089 |