Soluble T cell receptor-like properties of an HLA-B35-specific monoclonal antibody (TU165).
A mouse monoclonal antibody of IgM class (TU165) 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 TU165 recognized the HLA-B35 molecule. In a panel of 89 EBV-transformed lymphoblastoid cell lines, all HLA-B35+ cells (n = 24) reacted with TU165 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 TU165 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 beta 2-microglobulin genomic DNA into mouse P815 cells led to high expression of HLA-B molecules; yet, expression of the TU165 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 TU165.
Uchańska-Ziegler
B
B
Institut für Experimentelle Onkologie und Transplantationsmedizin, Universitätsklinikum Rudolf Virchow, Freie Universität Berlin, FRG.
Nössner
E
E
Schenk
A
A
Ziegler
A
A
Schendel
D J
DJ
D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D002460:Cell Line; D015797:HLA-B35 Antigen / Q000276:immunology*; D006801:Humans; D066298:In Vitro Techniques; D016254:Mutagenesis, Insertional; D010455:Peptides / Q000276:immunology; D011948:Receptors, Antigen, T-Cell / Q000276:immunology*
D000911:Antibodies, Monoclonal; D015797:HLA-B35 Antigen; D010455:Peptides; D011948:Receptors, Antigen, T-Cell