Soluble T cell receptor‐like properties of an HLA‐B35‐specific monoclonal antibody (TÜ165)

Uchańska-Ziegler, Barbara; Nößner, Elfriede; Schenk, Andrea; Ziegler, Andreas; Schendel, Dolores J.

doi:10.1002/eji.1830230325

Cited by 34 publications

(16 citation statements)

References 45 publications

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“…The first of the mAbs, W6/32HL, is a well-known antibody directed at a non-polymorphic framework determinant of all HLA class I molecules that are complexed to β 2 -m ( Barnstable et al 1978). The second is TÜ149 (Uchanska-Ziegler et al 1993), which has a reactivity for HLA-B, -C, and some -A molecules that are complexed with β 2 -m. The third antibody, HCA2, which was originally described by Stam et al (1990) as detecting HLA-A heavy chains, has recently been further characterized (Grandea et al 1995). To confirm its reactivity with HLA-G heavy chains, in addition to HLA-A heavy chains, we determined the reaction pattern of HCA2 by using onedimensional isoelectric focusing (IEF) of lysates from LG-2, JAR, and JEG-3 cells, followed by Western blotting.…”

Section: Antibodiesmentioning

confidence: 99%

“…Ag4-1 myeloma cells (Köhler et al1976;Uchanska-Ziegler et al 1993) with spleen cells from a female BALB/c mouse immunized with phytohemagglutinin-activated T cells from a healthy individual; differential screening was performed on a panel of hematopoietic cell lines. TÜ155 was determined to be an IgM and apparently reacts only with HLA-A molecules.…”

Section: Antibodiesmentioning

confidence: 99%

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Expression of HLA class I molecules in human first trimester and term placenta trophoblast

Hutter

Hammer

Blaschitz

et al. 1996

Cell and Tissue Research

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Expression of HLA class I molecules in trophoblast cells from various locations in normal human first trimester and term placenta was investigated by immunohistochemistry with a panel of monoclonal antibodies against the heavy chains or complete HLA class I molecules complexed with beta2-microglobulin. These reagents were also employed to distinguish between the products of different HLA class I loci. In addition to previously characterized reagents, a novel monoclonal antibody against HLA-A molecules (TU155) was used. Various choriocarcinoma and transfected cell lines served as controls for the specificities of the monoclonal antibodies. Cells in close contact with maternal cells, such as invading trophoblast cells and cells of the basal plate, expressed beta2-m micro globulin in association with HLA-G and HLA-C heavy chains. These class I heavy chains may also have been present as isolated molecules, although not in each of the cells. In contrast, cells of the chorion laeve exclusively expressed HLA-G, and not HLA-A, -B, or -C antigens. Our data support the often discussed immune protective function and the regulatory function of the HLA-G molecule, during invasion. In addition, by using monoclonal antibodies HCA2 (anti-HLA-A and -G), HC10 (anti-HLA-B and -C), TU149 (anti-HLA-B, -C, and some -A alleles), SFR8-B6 (anti-HLA-Bw6 and some -C), LA45 (some HLA-A and -B), TU48 (anti-HLA-Bw4 and some -A), and TU155 (anti-HLA-A), we show the presence of HLA-C molecules in all extravillous trophoblast cells of the cell columns and in the basal plate; the trophoblast cells of the chorion laeve lack this antigen. The function of this molecule is not clear, although a protective function against natural killer cell activity in the endometrium is postulated.

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Section: Antibodiesmentioning

confidence: 99%

Section: Antibodiesmentioning

confidence: 99%

Expression of HLA class I molecules in human first trimester and term placenta trophoblast

Hutter

Hammer

Blaschitz

et al. 1996

Cell and Tissue Research

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“…The unexpected high frequency of these antibodies and the ability to isolate several different antibodies directed to either complex is even more surprising in view of previous reports, in which the use of immunized or naive phage libraries resulted in only a single antibody clone [28,29,[46][47][48][49][50][51][52][53][54][55]. It would have been possible that one particular antibody family or antibody V gene segment would have an intrinsic propensity to bind HLA-A2 molecules, and that the high frequency could be explained by a high abundance of such antibodies in the nonimmune library.…”

Section: Strategies To Generate Antibodies With Tcr-like Specificitiesmentioning

confidence: 84%

“…Antibodies with the MHC-restricted specificity of T-cells are rare and have been difficult to generate by conventional hybridoma techniques because B-cells are not educated to be self-MHC restricted [24][25][26][27]52,54]. TCRs recognize intracellularly processed linear peptide antigens in the context of MHC molecules.…”

Section: Antibodies With Mhc-restricted Peptide-specific Binding: Tcmentioning

confidence: 99%

T-cell receptor-like antibodies: novel reagents for clinical cancer immunology and immunotherapy

Noy

Eppel

Haus-Cohen

et al. 2005

Expert Review of Anticancer Therapy

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Major histocompatibility complex class I molecules play a central role in the immune response against a variety of cells that have undergone malignant transformation by shaping the T-cell repertoire and presenting peptide antigens from endogeneous antigens to CD8+ cytotoxic T-cells. Diseased tumor or virus-infected cells are present on class I major histocompatibility complex molecule peptides that are derived from tumor-associated antigens or viral-derived proteins. Due to their unique specificity, such major histocompatibility complex-peptide complexes are a desirable target for novel approaches in immunotherapy. Targeted delivery of toxins or other cytotoxic drugs to cells which express specific major histocompatibility complex-peptide complexes that are involved in the immune response against cancer or viral infections would allow for a specific immunotherapeutic treatment of these diseases. It has recently been demonstrated that antibodies with the antigen-specific, major histocompatibility complex-restricted specificity of T-cells can be generated by taking advantage of the selection power of phage display technology. In addition to their tumor targeting capabilities, antibodies that mimic the fine specificity of T-cell receptors can serve as valuable research reagents that enable study of human class I peptide-major histocompatibility complex ligand presentation, as well as T-cell receptor peptide-major histocompatibility complex interactions. T-cell receptor-like antibody molecules may prove to be useful tools for studying major histocompatibility complex class I antigen presentation in health and disease as well as for therapeutic purposes in cancer, infectious diseases and autoimmune disorders.

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“…Some of these reagents were Abs that were generated in an MHC-restricted fashion against tumor Ags (62,63) or against the H-Y Ag (64). Other groups have demonstrated that particular mAbs recognize only a subset of the MHC molecules to which they were directed, and have suggested that such restricted reactivity was due to peptide specificity (65)(66)(67)(68).…”

Section: Discussionmentioning

confidence: 99%

Antibodies Directed Against the MHC-I Molecule H-2Dd Complexed with an Antigenic Peptide: Similarities to a T Cell Receptor with the Same Specificity

Poláková

Plaksin

Chung

et al. 2000

The Journal of Immunology

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αβ TCRs, which use an Ab-like structure to form a combining site, recognize molecular complexes consisting of peptides bound to MHC class I (MHC-I) or class II (MHC-II) molecules. To explore the similarities and differences between Ab and T cell recognition of similar structures, we have isolated two mAbs, KP14 and KP15, that specifically bind H-2Dd complexed with an HIV envelope gp160-derived peptide, P18-I10. These Abs are MHC and peptide specific. Fine specificity of mAb binding was analyzed using a panel of synthetic peptides, revealing similarities between the mAb and a cloned TCR with the same specificity. These two mAbs used the same VH and JH gene segments, but different D, Vκ, and Jκ genes. Administered in vivo, mAb KP15 blocked the induction of CTL specific for recombinant vaccinia virus-encoded gp160, indicating its ability to bind endogenously generated MHC/peptide complexes. Analysis of the fine specificity of these mAbs in the context of their encoded amino acid sequences and the known three-dimensional structure of the H-2Dd/P18-I10 complex suggests that they bind in an orientation similar to that of the TCR. Thus, the plasticity of the B cell receptor repertoire and the structural similarities among BCR and TCR allow Abs to effectively mimic αβ TCRs. Such mAbs may be useful in the therapeutic modulation of immune responses against infectious agents or harmful self Ags as well as in tracing steps in Ag processing.

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Soluble T cell receptor‐like properties of an HLA‐B35‐specific monoclonal antibody (TÜ165)

Cited by 34 publications

References 45 publications

Expression of HLA class I molecules in human first trimester and term placenta trophoblast

Expression of HLA class I molecules in human first trimester and term placenta trophoblast

T-cell receptor-like antibodies: novel reagents for clinical cancer immunology and immunotherapy

Antibodies Directed Against the MHC-I Molecule H-2Dd Complexed with an Antigenic Peptide: Similarities to a T Cell Receptor with the Same Specificity

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