Article

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

  1. Barbara Uchańska-Ziegler1,
  2. Elfriede Nößner2,†,
  3. Andrea Schenk1,
  4. Andreas Ziegler2,*,
  5. Dolores J. Schendel3

Article first published online: 9 DEC 2005

DOI: 10.1002/eji.1830230325

Issue

European Journal of Immunology

European Journal of Immunology

Volume 23, Issue 3, pages 734–738, March 1993

Additional Information

How to Cite

Uchańska-Ziegler, B., Nößner, E., Schenk, A., Ziegler, A. and Schendel, D. J. (1993), Soluble T cell receptor-like properties of an HLA-B35-specific monoclonal antibody (TÜ165). Eur. J. Immunol., 23: 734–738. doi: 10.1002/eji.1830230325

Author Information

  1. 1

    Institut für Experimentelle Onkologie und Transplantationsmedizin, Universitätsklinikum Rudolf Virchow, Freie Universität Berlin, Berlin

  2. 2

    Institut für Immunologic, Universität München, München

  3. 3

    Medizinisch-Naturwissenschaftliches Forschungszentrum, Universität Tübingen, Tübingen

  1. †

    Department of Cell Biology, Stanford University, Palo Alto, USA

*Institut für Experimentelle Onkologie und Transplantationsmedizin, Universitätsklinikum Rudolf Virchow, Freie Universität Berlin, Spandauer Damm 130, D-1000 Berlin 19, FRG

Publication History

  1. Issue published online: 9 DEC 2005
  2. Article first published online: 9 DEC 2005
  3. Manuscript Revised: 26 NOV 1992
  4. Manuscript Received: 15 OCT 1992

Funded by

  • Deutsche Forschungsgemeinschaft. Grant Numbers: 120, 217, Zi 268/1-1
  • Berliner Krebsgesellschaft

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Keywords:

  • Peptide-MHC complex;
  • HLA-B35;
  • Epstein-Barr virus;
  • T cell receptor;
  • Monoclonal antibody

Abstract

A mouse monoclonal antibody of IgM class (TÜ165) was produced using Epstein-Barr virus (EBV)-infected mutant cells derived from the human BJAB-B95.8.6 cell line as immunogen. Binding studies with several HLA deletion mutant cell lines indicated that TÜ165 recognized the HLA-B35 molecule. In a panel of 89 EBV-transformed lymphoblastoid cell lines, all HLA-B35+ cells (n = 24) reacted with TÜ165 while all but two HLA-B35− lines (n = 65) were unreactive (r = 0.95). Surprisingly, peripheral blood lymphocytes of HLA-B35+ donors were unreactive; however, strong enhancement of TÜ165 recognition was observed with B cells of one of these individuals after transformation with EBV (B95.8 strain). Transfection of both HLA-B35 and human ß-microglobulin genomic DNA into mouse P815 cells led to high expression of HLA-B molecules; yet, expression of the TÜ165 epitope was not observed. Furthermore, the EBV-negative cell line BJAB as well as the EBV-infected (P3HR1 strain) line BJAB-HR1K were only weakly reactive, whereas the BJAB-B95.8 cell line was strongly positive. These results indicate that EBV-encoded or -controlled peptide(s) must be bound by HLA-B35 antigens to create the epitope which allows efficient binding of TÜ165.

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