Use of Monoclonal Anti-mouse Immunoglobulin to Detect Mouse Antibodies

Yelton, Dale E.; Desaymard, Catherine; Scharff, Matthew D.

doi:10.1089/hyb.1.1981.1.5

Cited by 244 publications

(90 citation statements)

References 8 publications

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“…K562 cells transfected with full-length, wild-type ␣ 3 (K562-␣ 3 WT) and ␣ 6 (K562-␣ 6 WT) subunits were described previously (31,32). The following monoclonal antibodies were used in this study: anti-integrin ␣ 2 , A2-IIE10 (33); anti-integrin ␣ 3 , A3-IVA5 and A3-IIF5 (31); anti-integrin ␣ 6 , A6-ELE (34); anti-integrin ␤ 1 , TS2/16 (35); anti-CD151, 5C11 (28), 11B1 (36), and TS151r (29); anti-CD81, M38 (37); anti-CD9, DU-ALL (Sigma); anti-HA (Berkeley Antibody Co., Richmond, CA); anti-vinculin (Sigma); and negative control antibodies, 187.1 (38) and J2A2 (39). Unless otherwise indicated, mAb 5C11 was used for all CD151 immunoprecipitations, and mAb 11B1 was used for all CD151 immunoblots.…”

Section: Methodsmentioning

confidence: 99%

Direct Extracellular Contact between Integrin α3β1 and TM4SF Protein CD151

Yauch¹,

Kazarov²,

Desai³

et al. 2000

Journal of Biological Chemistry

181

163

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Previously we established that the ␣ 3 ␤ 1 integrin shows stable, specific, and stoichiometric association with the TM4SF (tetraspannin) protein CD151. Here we used a membrane impermeable cross-linking agent to show a direct association between extracellular domains of ␣ 3 ␤ 1 and CD151. The ␣ 3 ␤ 1 ؊CD151 association site was then mapped using chimeric ␣ 6 /␣ 3 integrins and CD151/NAG2 TM4SF proteins. Complex formation required an extracellular ␣ 3 site (amino acids (aa) 570 -705) not previously known to be involved in specific integrin contacts with other proteins and a region (aa 186 -217) within the large extracellular loop of CD151. Notably, the anti-CD151 monoclonal antibody TS151r binding epitope, previously implicated in ␣ 3 integrin association, was mapped to the same region of CD151 (aa 186 -217). Finally, we demonstrated that both NH 2 -and COOH-terminal domains of CD151 are located on the inside of the plasma membrane, thus confirming a long suspected model of TM4SF protein topology.

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Section: Methodsmentioning

confidence: 99%

Direct Extracellular Contact between Integrin α3β1 and TM4SF Protein CD151

Yauch¹,

Kazarov²,

Desai³

et al. 2000

Journal of Biological Chemistry

181

163

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“…The level of serum anti-M and anti-NP antibodies was determined by radioimmunoassay (RIA) as described (28). Briefly, wells of a 96-well polyvinyl microtiter plate were coated with purified M (-250 ng per well) or NP (-200 ng per well) and developed with the iodinated rat anti-mouse K-light-chain constant region (CK) monoclonal antibody, antibody 187.1 (29). The antibody response to core proteins was measured in an ELISA.…”

Section: Methodsmentioning

confidence: 99%

Differential ability of B cells specific for external vs. internal influenza virus proteins to respond to help from influenza virus-specific T-cell clones in vivo.

Scherle

Gerhard

1988

Proc. Natl. Acad. Sci. U.S.A.

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When a helper T-cell (TH) clone specific for the hemagglutinin, neuraminidase, matrix protein, or nucleoprotein of influenza strain A/PR/8/34 is adoptively transferred to athymic mice 1 day after virus infection the anti-viral antibody response of the mouse is enhanced. This response is directed predominantly to the hemagglutinin and requires associative T-cell-B-cell interactions. Delaying For a resting B cell to become activated and produce antibodies, a second signal, beyond the occupancy of its surface immunoglobulin receptor by antigen, is required (1, 2). This signal is in most cases provided by helper T cells (TH). Two types of T-cell help have been described (3, 4).Cognate help is major histocompatibility complex-restricted and requires that the antigenic determinants recognized by the B cell and by the T cell be covalently linked (5)(6)(7)(8). This type of help is thought to occur through a direct interaction between the TH and B cells and to result in the transduction of a signal to the B cell in the form of locally released factors and/or crosslinking of surface molecules. This signal enables the B cell to go on to proliferate and differentiate into an antibody-secreting B-cell clone (9-13). Bystander help, in contrast to cognate help, is thought to occur through the release of T-cell-derived factors that act nonspecifically on activated B cells (14)(15)(16)(17). No direct link between the antigenic determinants recognized by the T cell and the B cell is, therefore, required. 4446The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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“…A total of 95% to 98% of normal murine B cells expressed light chain as shown previously. 25 Normal B cells also expressed CD19, and in contrast to 38c13 they also expressed B220. 26 Mice were irradiated and injected intraperitoneally with lymphoma cells.…”

Section: Anti-cd19-car-transduced T Cells Eradicated Both Lymphoma Cementioning

confidence: 98%

Adoptive transfer of syngeneic T cells transduced with a chimeric antigen receptor that recognizes murine CD19 can eradicate lymphoma and normal B cells

Kochenderfer

Frasheri

et al. 2010

Blood

315

261

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Adoptive T-cell therapy with anti-CD19 chimeric antigen receptor (CAR)–expressing T cells is a new approach for treating advanced B-cell malignancies. To evaluate anti-CD19–CAR-transduced T cells in a murine model of adoptive T-cell therapy, we developed a CAR that specifically recognized murine CD19. We used T cells that were retrovirally transduced with this CAR to treat mice bearing a syngeneic lymphoma that naturally expressed the self-antigen murine CD19. One infusion of anti-CD19–CAR-transduced T cells completely eliminated normal B cells from mice for at least 143 days. Anti-CD19–CAR-transduced T cells eradicated intraperitoneally injected lymphoma cells and large subcutaneous lymphoma masses. The antilymphoma efficacy of anti-CD19–CAR-transduced T cells was critically dependent on irradiation of mice before anti-CD19–CAR-transduced T-cell infusion. Anti-CD19–CAR-transduced T cells had superior antilymphoma efficacy compared with the anti-CD19 monoclonal antibody from which the anti-CD19 CAR was derived. Our results demonstrated impressive antilymphoma activity and profound destruction of normal B cells caused by anti-CD19–CAR-transduced T cells in a clinically relevant murine model.

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Use of Monoclonal Anti-mouse Immunoglobulin to Detect Mouse Antibodies

Cited by 244 publications

References 8 publications

Direct Extracellular Contact between Integrin α3β1 and TM4SF Protein CD151

Direct Extracellular Contact between Integrin α3β1 and TM4SF Protein CD151

Differential ability of B cells specific for external vs. internal influenza virus proteins to respond to help from influenza virus-specific T-cell clones in vivo.

Adoptive transfer of syngeneic T cells transduced with a chimeric antigen receptor that recognizes murine CD19 can eradicate lymphoma and normal B cells

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